aceK

Isocitrate dehydrogenase kinase/phosphatase

625 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

72.902 kDa

MFPQRLDSTIAYDIAKAMMDGFNRHYQLFRTESARAKHRFETADWHGQQRAQRERIEFYDLRVREASTRLEREFKAGEQSMDVWHQVKLHYIGLLVNHHQPELAETFFNSVTTKILHRSYFQNDFIFVRPAVSTEYIENEEPTAQPTYRAYYPTRDNLREIIVRLVRDFDLRLEFEDLERDAGYVLEAVSERLSDVKLRANFQIQVLSGLFFRNKGAYVVGKIINGFNEVPLALPILHSKSGKLVIDAALFGEDDLLILFSFARAYFMVDMGIPSAYVQFLRSMMPHMPRAEIYNALGLAKQGKTLFYRDFLHHLRHSTDKFRIAPGIKGMVMLVFDLPSFPYVFKVIKDYYPPQKDTSREQIKGKYLLVKQHDRVGRMADTQEYSEVAFPRARFDDELIAEIEKFAPSQLEISDRDRDGNTEVIIKHVYIERRMIPLNIYLQEAFDAGVGEPAAKNQIERAVVEYGNAIKDLVAANIFPGDMLWKNFGITRHGKVVFYDYDEIEYITDCKFRRVPAPRNDEEEMSGEVWYSVGPKDVFPETFAPFLLGNDAVREVFMKHHGDLLDAEFWQSHQARIQAGHVHDVFPYEREKRFTRRHSPGRNDHELLTHLPPEPMLTGLSGMTP

aceK

Isocitrate dehydrogenase kinase/phosphatase

623 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

72.058 kDa

MFPQRLDSTVAYAIAKAMIDGFNRHYRLFRTESARAKHRFETADWHGQQRAQRERIEFYDLRVREASIRLEREFKAGEQPMDVWHQVKLHYIGLLVNHHQPELAETFFNSVTTKILHRSYFQNDFIFVRPAVSTEYIENQEPTAQPTYRAYYPTQGNMHETLVKLVEDFGLCREFEDLRRDAGYVAEAMAARLGDVKLRANFQIQVLSGLFFRNKGAYVVGKIINGFGEIPFALPILHRQPAPGQVLPADGKGISSQSDAGKLVIDAALFGEDDLLILFSFARAYFMVDMGIPSAFVQFLRSMMPRMPRAEIYNALGLAKQGKTLFYRDFLHHLRHSTDKFRIAPGIKGMVMLVFDLPSFPYVFKVIKDYYPPQKDTTREQIKGKYLLVKQHDRVGRMADTQEYSEVAFPRERFSDELIAEIEKFAPSQLEISDRDGDGQMEVIIKHVYIERRMIPLNIYLQEAFDFGVAEPAARDQIERAVVEYGNAIKDMVAANIFPGDMLWKNFGITRHGKVVFYDYDEIEYITDCKFRKVPTPRNEEDEMSGEVWYSVGPKDVFPETFGPFLLGNDAVREVFMKHHADLLDAAFWQRHQARIQAGHVYDVFPYDQQKRFAVMHGPARAG

aceK

Isocitrate dehydrogenase kinase/phosphatase

619 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

70.681 kDa

MIYSGDVQRIEPAPVAGPAPLDVAHLILAGFDRHYALFRYSAQRAKSLFESGDWHGMQRLSRERIEYYDMRVRECATQLDSALRGSDARTADGSRANGSAALSEAQTAFWQAVKQEFVGLLADHRQPECAETFFNSVSCRILHRDYFHNDFLFVRPAIATDYLDSRIPSYRVYYPVAEGLHKSLIRMVADFGLAVPYADLPRDARLLARAAVRQLRGQLPRHAGPRLASDCQIQVLGSLFFRNTGAYIVGRLINQGTVYPFAVALRRNPAGQVCLDALLLGADDLSTLFSFTRAYFLVDMETPAAVVNFLASLLPRKPKAELYTMLGLQKQGKTLFYRDFLHHLTHSRDAFDIAPGIRGMVMCVFTLPSYPYVFKLIKDRIDKDGMDHATVRRKYQMVKLHDRVGRMADTWEYSQVALPRSRFAPRLLEELRRLVPSLIEENGDTVVIRHVYIERRMMPLNLYLRHASDPLLEVAVREYGDAIRQLATANIFPGDMLYKNFGVTRLGRVVFYDYDEIQRMTEMNFRAIPPAPNEEAELSSEPWYAVGPNDVFPEEFGRFLLGDPRVRQAFLRHHADLLAPQWWQACRARVAQGRIEEFFPYDTDRRLHPQAAPPPRTAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

618 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

72.031 kDa

MAGSFVTTLNDPRAFDIAQALLDGFNRHYKLFRQTSAEAKQRFEAADWHGQQRAQRERIEFYDLRVDEAAERLENEFRASSLSEETWQQVKLYYIGLLINHHQPELAETFFNSVTTKILHRSYFRNDFIFVRPAVSTEYIENEEPDSLPTYRAYYPSRPGSAEGLRETLLRIVDNYQLQREFEDLGRDIDYVLQAFRNQFGDVKLSANFQIQVLASLFFRNKGAYIVGKVINGFRETGFALPVLHNSRELLTIDTALFGEDELLLLFSFARAYFLVDMEIPSAYVQFLRSLMPRKPRWELYNALGLQKQGKNQFYRDFLYHLRHSSDSFRIAPGIKGMVMLVFDLPSFPFVFKVIKDFYPPQKDTTRELIQSKYQLVKTHDRVGRMADSLEYSNVAFPRQRFEPELIEEIRHFCPSLLEEEGDSLVLKHLYIERRMIPLNIYLQEATPEQMKHAVIEYGNAIKDLVAANIFPGDMLWKNFGVTRHGKVVFYDYDEIEYLTDCNFRKVPEPRTEEEEMSGDIWYSVGPKDVFPETFGPFLLGNPTVREVFMQHHAELLDPAFWQGRKDRIAGGYVHDVFPYDPHKRFRRPLGLGFGSLDAEAVSLHPASATTQLGHNPI

aceK

Isocitrate dehydrogenase kinase/phosphatase

615 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

71.671 kDa

MSHFPKLLSSQIAYDVARTMLDGFDKHYRLFREVSHQAKLKFEAGDWHGLQQIQRDRIAFYNERVRESSVILEDEYDAENIEDEIWQQIKLHYIGLLTNHHQPELAETFFNSVCTRILHRSYFNNDFIFVRPAISTEYIENEESPTRPTFRAYYPGSREGMAACFERIVHNFQLERPFEDLQRDIGYVVRAVGEHFGDLRIAPNFQIHTLSSLFFRNKAAFIIGRILNGDRTFPLAIPILHGPSGKLVLDTVLLKKEQLLILFSFTHSYFMVDMEIPSAYVTFLRDIMPRKPRAEIYTSLGLQKQGKNLFYRDFLHHLQHSSDKFIVAPGIRGLVMLVFTLPSYPYVFKVIRDVFPAPKETTRELVKSKYQLVKQHDRVGRMADTLEYSDVAFPLSRFDEALVREFEQHAPSMIEYQRAKDGGEEIVVRHVYIERRMTPLNIYLQEGSDAQVEHGVIEYGNAIKELIAANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNIRHVPQPRNEEEEMSGEVWYTVRPHDIFPETFRTFLLGDPRVGAAFLRHHADFFDPAMWQSHKDRLLAGHVHDFFAYHASDRFIHRYGAAAEPPATPPVKQPDAGPARRVA

aceK

Isocitrate dehydrogenase kinase/phosphatase

615 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

71.666 kDa

MFPTRLDSSLAYDIAKAMMDGFNRHYRLFRTESARAKHRFETADWHGQQRAQRDRIEFYDLRVRECFMRLAREFKADEQPMEVWQQVKLHYIGLLVDHHQPELAETFFNSVTTKILHHSYFQNDFIFVRPAVSTEYIENDESETSPTYRSYYPTHDSLAEVLVQMVLDFDLRCPFADLDSDAARVQAAMVEQLGEVKLRANFQLQVLSGLFFRNKGCYIVGKLINGFNEFPFALPVLYGRAGQLVIDAVLFGEDDLLMLFSFARAYFMVDMEIPSAYVQYLRSMMPRKPRNEIYNALGLAKQGKTLFYRDFLHHQRHSTDKFRIAPGIKGMVMLVFDLPSFPYVFKVIKDFYPPPKDTTREQIKAKYLLVKQHDRVGRMADTLEYSEVGFPRARFDDELIAELEKFAPSQLEISDRDGDGRIEVIIKHVYIERRMIPLNIYLQEAFDAGGANPDDTSPAALRAREQIERGVIEYGNALKDLVAANIFPGDMLWKNFGITRHGKVVFYDYDEIEYITDCNFRKVPQARNEEDEMSGEVWYRVGPKDVFPETFAPFLLGNPFVREVFMKHHAELLDAAFWQSHKERIQAGHVYDVFPYDQGKRFHPEISDAQVPSSI

aceK

Isocitrate dehydrogenase kinase/phosphatase

613 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

71.48 kDa

MSHFPKLLSSQIAFDVARTMLDGFDKHYRLFREVSHQAKLKFEAGDWHGLQQIQRDRIAFYNERVRESSVILEDEYDAENIEDEIWQQIKLHYIGLLTNHHQPELAETFFNSVCTRILHRSYFNNDFIFVRPAISTEYIENEESPTRPTFRAYYPGSREGMAACFERVVHNFQLESPFEDLQRDIGYVVRAVSEHFGDLRIAPNFQVHTLSSLFFRNKSAFIIGRILNGDRTFPLAIPIVHGPSGKLTLDTVLLKKEQLLILFSFTHSYFMVDMEIPSAYVTFLRDIMPRKPRAEIYTSLGLQKQGKNLFYRDFLHHLQHSSDKFIVAPGIRGLVMLVFTLPSYPYVFKVIKDFFPAPKETTRELVKSKYQLVKQHDRVGRMADTLEYSDVAFPLSRFDEALVREFEQHAPSMIEYQRGKDGGEEIVVRHVYIERRMTPLNIYLTEGTDEQVEHGVIEYGNAVKELIAANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNIRDVPQPRNEEEEMSGEVWYTVRPHDIFPETFRTFLLGDTRVRAAFLRHHADFFDPAMWQSHKDRLLAGHVHDFFAYHSSERFIHRYSEAGSAQGTAAVPDPGPARRVA

aceK

Isocitrate dehydrogenase kinase/phosphatase

612 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

70.624 kDa

MNHFPKLLSSQIGFDLAQTMLEGFDRHYRIFRDAAIHAKTLFEKGDWHGLQKLARDRITSYDERVDECVELLEDEYDAEKIDSEVWQQIKLHYIGLLTTHRQPECAETFFNSVCCKILHRSYFNNDFIFVRPAISTEYIENDEPAAKPTYRAYYPGKDGLAATLERIVTNFQLEPQFEDLTRDVGCVMQAIHDAFGAFDEAPNFQIHVLSSLFYRNKSAYIVGRIINGDLLLPFAVPLRHVKPGVLALDTVLLKREQLLIIFSFSHSYFLVDMEVPSAYVEFLGTIMPGKPKAEIYTSVGLQKQGKNLFYRDLLHHLSHSSDQFIIAPGIKGLVMLVFTLPSFPYVFKLIKDNFPPPKETTRAQIQSKYQLVKRHDRLGRMADTLEYSSVALPRSRLDDALVRELEKEVPSLLEYEGENLVIRHMYIERRMVPLNLFLQNGNDEDVEHGIKEYGNAVKELMQANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRAVPAPRNEEDEMSGEPWYSVGPHDIFPETYGTFLLGDPRVRRSFMQHHADFFDPALWQRHKDHLLKGELPDFFPYDDSARFCNCYPERFADAAGRASPEPDAPADARSVRVA

aceK

Isocitrate dehydrogenase kinase/phosphatase

612 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

70.542 kDa

MNHFPKLLSSQIGFDVAQTMLEGFDRHYRIFRDAAIHAKTLFEQADWHGLQKLARDRITSYDERVEECVELLEDEYDAENIDDEVWQQIKLHYIGLLTTHRQPECAETFFNSVCCKILHRSYFSNDFIFVRPAISTEYIENDEPAAKPTYRAYYPGKDGLAATLERIVTNFQLEPPFEDLTRDVGCVMQAIQDAFGVFDEAPNFQIHVLSSLFYRNKSAYIIGRIINGDLLMPFAVPLRHVKPGVLALDTVLLKRDQLLIIFSFSHSYFLVDMEVPSAYVEFLGTIMQGKPKAEIYTSVGLQKQGKNLFYRDLLHHLSHSSDQFIIAPGIKGLVMLVFTLPSFPYVFKLIKDSFPPPKETTRAQIKEKYQLVKRHDRLGRMADTLEYSSVALPVSRLDEALVRELEKEVPSLIEYDGDSLVIRHMYIERRMVPLNLFLQNGNDEDIEHGIKEYGNAIKELMQANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRAVPAPRNEEDEMSGEPWYSVGPHDIFPETYGTFLLGDPRVRRSFMQHHADFFDPALWQRHKDHLLKGELADFFPYDGSVRFCMRYPERFADAAGAASNEQDAPDAGRSVRAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

611 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

71.186 kDa

MSHFPKLLSSQIAFDVARTMLDGFDKHYRLFREVSVQAKTAFETGDWAGLQQLQRDRIAYYDERVREASVILEDEYDAENIDDEIWRQIKLHFIGLLTNHHQPECAETFFNSVCTRILHRSYFNNDFIFVRPAISTEYIENEESPTKPTYRAYYPGTRDGLGACFERIVHNFQLNAPFEDLERDIGYVVRAVGEHFGDFRIAPNFQIHVLSSLFFRNKAAYIIGRVINGDKTFPLAVPILRNAAGQLSLDTVLLRQEQLLILFSFTHSYFMVDMEIPSAYVTFLRDLMPRKPRAEIYTSLGLQKQGKNLFYRDFLHHLQHSSDKFIIAPGIKGLVMLVFTLPSYPYVFKVIKDYFPPPKETTRELIKSKYQLVKRHDRVGRMADTLEYSDVAFPLSRFDDDLIKELEKHAPSMVEYQRSEDGGEEIVIRHVYIERRMTPLNIWLHEGTDAQVEHGIIEYGNAIKELIAANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNIRTVPEPRTEEEEMSGEVWYNVGPHDIFPETYRTFLLGDPRVREAFLKHHADFFEASMWQGYKERLLSGQMHDFYAYDAAERFVNRYGASAPDNAAQDNTTLQRAAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

610 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.975 kDa

MTATASHTRARPLGASEIEHATRIAEPDFDLLDALYRTDDPDDQARLLARVVLSAFDNYYAVSRRIPALAQAAFEARDWPVTVRLSKIRIGLYTACIDQLVPLLKAGLPELTTDEQLWPTAEAELLAAIEGRYEADFAFAFWQSLRRKLVSDEWRPVSYDAGSTARRTTSPAAVLKTTATTLPITAEVIAGILDEAGFRVPWRDRDGDAALAAQAIETALEPLSPRPGEPVKIEIADSGFLRNRGACLVGRIKLRDRGDMPMRNLPLLIALLNEKDGLVVDAVLTDSDELQYAFSSTLANYHATNPRYHELARLLYELMPKRPLGTQYSCIGFHHLGKVAVMSEILAEHRKTKEKLATAPGFKGTVAIAFTMPSSAYVLKIIRDHPTDDYKFDYFDGLDEVLRKYNLVHEIDRAGSMLDNIIYSNVKLDRAMFAPELLDELLEAGIGTVTLDRGALVFRHLIVQIKLTPLPLYLANASAAESRAAVINLGDCIKNNAAADIFNKDLDGRNYGVSRIRKVYLFDYDAVEPLTSVTVSRDGAAPGEFDNGMVFRPQEMLEGLRIDDPGLRRAFRDAHPELMQADYWEGMQQALRDGKVPKVMNYPASRRLRR

aceK

Isocitrate dehydrogenase kinase/phosphatase

610 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.979 kDa

MTATASHTRARPLGASEIEHATRIAEPDFDLLDALYRTDDPDDQARLLARVVLSAFDNYYAVSRRIPALAQAAFEARDWPVTVRLSKIRIGLYTACIDQLVPLLKAGLPELTTDEQLWPTAEAELLAAIEGRYEADFAFAFWQSLRRKLVSDEWRPVSYDAGSTARRTTSPAAVLKTTTTTLPITAEVIAGILGDAGFRVPWRDRDGDAALAAQAIETALEPLSPRPGEPVKIEIADAGFFRNRGACLVGRIQLRDRGDMPMRNLPLLIALLNEKDGLVVDAVLTDSDELQYAFSSTLANYHATNPRYHELARLLYELMPKRPLGTQYSCIGFHHLGKVAVMSEILAEHRKTKERLATAPGFKGTVAIAFTMPSSAYVLKIIRDHPTDDYKFDYFDGLDEVLRKYNLVHEIDRAGSMLDNIIYSNVKLDRAMFAPELLDELLEAGIGTVTLDRGALVFRHLIVQIKLTPLPLYLANASAAESRAAVINLGDCIKNNAAADIFNKDLDGRNYGVSRIRKVYLFDYDAVEPLTSVTVSRDGAAPGEFDNGMVFRPQEMLEGLRIDDPGLRRAFRDAHPELMQADYWEGMQRALRDGKVPKVMNYPASRRLQR

aceK

Isocitrate dehydrogenase kinase/phosphatase

609 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

71.044 kDa

MFPERLDAPQAYDIAKAMMDGFNRHYRLFRAESARAKHRFETADWHGQQRAQRERIEFYDLRVRECVRRLDKEFNAGALPMDVWHQIKLHYIGLMVNHLQPELAETFFNSVTTKILHRTHFHNDFIFVRPAVSTEYIESDDPGARPTYRAYYPSRDNLHETVVRIVEHCALQRDFENLPRDAGHVVQALQQRLGAVKLRTNFQVQVLSSLFFRNKGAYLVGKVINGYNELPFALPILHGEDGRLLIDAVLFGENDLQMLFSFARAYFMVDMEIPSAYVQFLRSLMPRKPRAELYTALGLAKQGKTLFYRDFLHHLRYSTDKFRIAPGIKGMVMLVFDLPSFPYVFKLIKDQFPAPKDTTREQVQGKYLLVKQHDRVGRMADTLEYSLVAFPRERFSDELIEEIRRHAPSQIEISDRDGDGRQEVIIAHLYIERRMIPLNIHLQECFDTGLDKPEARSALEHAVTEYGNAIKDMVAANIFPGDMLWKNFGITRNGKVVFYDYDEIEYLTDCNFRRVPPPRCEEDEVSGEVWWPVGPHDVFPETFGPFLLGNDSVREAFMRHHADLLDVEFWQSHKERIQAGHLYDVFPYDSARRFRCASPSSFQTQGDST

aceK

Isocitrate dehydrogenase kinase/phosphatase

608 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

71.455 kDa

MSHFPKLLSSQIAFDVARTMLDGFDKHYRLFREVSRQAKVKFEAGDWHSLQQMQRDRIAFYNERVRETSVILEDEYDAENIEDEIWQQIKLHYIGLLTNHHQPELAETFFNSVCTRLLHRSYFNNDFIFVRPAISTEYIENEESPTRPTFRAYYPGSRQGMAECFERIVHNFQLETPFEDLRRDVGHVVRGVEEHFGDFRIAPNFQIHVLSSLFFRNKTAFIIGRIVNADRTYPLAIPIVHGPSGKLTLDAVLLKKVQVLILFSFTHSYFMVDMEIPSAYVTFLRDIMPRKPRAEIYTSLGLQKQGKNLFYRDFLHHLQHSSDKFISAPGIKGLVMLVFTLPSYPYVFKVIKDFYPAPKETTRELIKSKYQLVKQHDRVGRMADTLEYSNVAFPLSRFDEDLVRELEHHAPSMIEYQRGKDGGEEIVVRHVYIERRMTPLNIWLQEGTDEQLEHGIIEYGNAIKELIAANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYFTDCNVRRVPQPRNEEEEMSGDIWYTVRPHDIFPETFRTFLLGNPRVREAFLRHHEDLFDPAMWQSHKDRLLAGHVHDFFAYPISERFINRYGTAAHGTPVASFARRVA

aceK

Isocitrate dehydrogenase kinase/phosphatase

608 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

70.553 kDa

MSHFPKLLSSQIAFDVARTMLDGFDKHYRLFREVSVRAKALFEAGDWQGLQQLQRDRIAYYDERVREASVILEDEYDAENIDDEIWRQIKLHFIGLLTNHHQPECAETFFNSVCTRILHRSYFNNDFIFLRPAISTEYIENEESPTKPTYRAYYPGSREGLGGCLERIVHNFQLDAPFEDLPRDIGYVVRAVGEHFGDFRIAPNFQIHVLSSLFFRNTAAYIIGRVINGDKTYPLAVPIMRGADGQLRLDTVLLRPEQLLILFSFTHSYFMVDMEIPSAYVTFLRDLMPRKPRAEIYTSLGLQKQGKNLFYRDFLHHLQHSSDKFIIAPGIKGLVMLVFTLPSYPYVFKVIKDYFPPPKETTRELIKSKYQLVKQHDRVGRMADTLEYSDVAFPLSRFDDALIKELEKHAPSMVEYQRGADGSDEIVIRHVYIERRMTPLNIWLHEGTDAQVEHGIIEYGNAIKELIAANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRDVPQPRNEEEEMSGEVWYSVGPHDIFPQTYGTFLLGDPRVREAFLRHHADFFDPAMWQAHKARLLSGQTHDFYAYDASERFVNRYGDSAPGNAATPLRRAAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

608 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

70.263 kDa

MNHFPKLLSSQIGFDVAQTMLENFDRHYRIFREAAVDAKTLYERADWHGLQRLARERITSYDDRVQECVEVLQDEYDAENIDDEVWQQIKLHYIGLLTSHRQPECAETFFNSVCCKILHRSYFNNDFIFVRPAISTEYLENDEPAAKPTYRAYYPGTDGLAATLERIVTNFQLEPPFEDLTRDIGCVMQAITDEFGEFDAAPNFQIHVLSSLFFRNKSAYIVGRIINADRVLPFAVPIRHVRPGLLALDTVLLRRDLLQIIFSFSHSYFLVDMGVPSAYVDFLCTIMPGKPKAEIYTSVGLQKQGKNLFYRDLLHHLSHSSDRFIIAPGIKGLVMLVFTLPSFPYVFKIIKDHFPPPKETTREQIMEKYQLVKRHDRLGRMADTLEYSSVALPISRLDHALVRELEKEVPSLLEYEDGNLVIKHLYIERRMIPLNLYLQNGTDAEIEHGVKEYGNAVKELMKANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRRVPPPRNEEDELSGEPWYTVGPHDIFPETYGPFLLGDPRVRAVFMKHHADFFEASLWQASKDKLLQGELPDFYPYDVSLRFSVRYPDRFDSTPDAGDGDSAGDAQRAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

608 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

70.231 kDa

MNHFPKLLSSQIGFDVAQTMLENFDRHYRIFREAAVDAKTLYERADWHGLQRLARERITSYDDRVQECVEVLQDEYDAENIDDEVWQQIKLHYIGLLTSHRQPECAETFFNSVCCKILHRSYFSNDFIFVRPAISTEYLENDEPAAKPTYRAYYPGTDGLAATLERIVTNFQLEPPFEDLTRDIGCVMQAITDEFGEFDAAPNFQIHVLSSLFFRNKSAYIVGRIINADRVLPFAVPIRHVRPGLLALDTLLLRRDLLQIIFSFSHSYFLVDMGVPSAYVEFLCTIMPGKPKAEIYTSVGLQKQGKNLFYRDLLHHLSHSSDRFIIAPGIKGLVMLVFTLPSFPYVFKIIKDHFPPPKETTREQIMEKYQLVKRHDRLGRMADTLEYSSVALPISRLDHALVRELEKEVPSLLEYEDGNLVIKHLYIERRMIPLNLYLQNGTDAEIEHGVKEYGNAVKELMKANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRRVPPPRNEEDELSGEPWYTVGPHDIFPETYGPFLLGDPRVRAVFMKHHADFFEASLWQASKDKLLQGELPDFFPYDVSLRFSVRYPDRFDATPDAGDGDSAGNAQRAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

607 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

71.11 kDa

MSHFPKLLSSQIAYDVARTMLDGFDKHYRLFREVSIEAKARFEVGDWHGLQQLQRDRIAFYNQRVHETIVTLQDEYDAEDIEDEIWQQIKLHYIGLLTNHHQPELAETFFNSVFTRIQHRSYFNNDFIFVRPAISTEYIENEESPIKPTYRAYYPGSREGMAACFERIVNNFQLERPFEDLKRDAGYVARAITEHFGEFRIAPNFQVHTLSSLFFRNKTAFVIGRVINGDHTYPLVVPIIHAASGKLVLDTVLLHREQILILFSFAHAYFMVDMEIPSAYVTFLRDLLPRKSRAEIYTSLGLQKQGKNLFYRDFLHHLQHSSDKFISAPGIKGLVMLVFTLPSFPYVFKVIRDFFPAPKETTRELVKSKYQLVKQHDRVGRMADTLEYSDVAFPLSRFDDALVRELEQHAPSMIEYQRSKQGEDEIVVRHVYIERRMTPLNIWLQEGTDEQVDHGILEYGNAVKELIAANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRRVPAPRNEEEEMSGEVWYTVRPHDIFPETYGTFLLGDPRVRAAFMRHHPDFFDAAMWQHHKDRLLAGHVHDFFAYHSQERFIHRYGSGATGPATEEPRRAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

606 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

70.106 kDa

MNHFPKLLSSQIGFDIAQTMLEYFDRHYRIFREAAVEAKTLYERGDWHGLQRLARERITSYDERVKECVELLEDEYDAENIDDEVWQQIKLHYIGLLTSHRQPECAETFFNSVCCKILHRSYFNNDFIFVRPAISTEYLENDEPAAKPTYRAYYPGTDGLAATLERIVTNFQLEPPFEDLTRDIGCVMQAIDDEFGQFDAAPDFQIHVLSSLFFRNKSAYIIGRIINADRVLPFAMPIRHVRAGVLAVDTVLLRRELLQVIFSFSHSYFLVDMGVPSAYVDFLCTIMPGKPKAEIYTSVGLQKQGKNLFYRDLLHHLSHSSDRFIIAPGIKGLVMLVFTLPSFPYVFKIIKDHFPPPKETTRAQIMEKYQLVKRHDRLGRMADTLEYSSVALPLSRLDHALVRELEKEVPSLLEHEDDNLVIEHLYIERRMTPLNLYLQNGSDADIEHGVKEYGNAVKELMKANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRRVPAPRNEEDELSGEPWYTVGPHDIFPETYGPFLLGDPRVRTVFMKHHADFFDPALWQASKDKLLQGELPDFYPYDTSLRFCVRYAARFDATPDHDDGAGAAQRAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

606 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.37 kDa

MTADAHLFSASDLEAATRIAEPDFELLDALIRTDDPDDQAHTLARVALSAFDNYYAVSRRIPALAKAAFYARDWPATVRLSKIRIGLYTACIDQLVPLLKAGLPELANDEQVWVRAEAELLAAIAGRYEADFAFAFWQSLRRKLVSDEWRPVSYDTGPAARPPAAIAAVVRTIAATLPIQPEVIRNVLDAAGFTGPWRDLDGDAALAAAAIEAALEPLSPRAGETAKIEIAESGFFRNRGACLVGRIRLRDRGDMPPRNIPLLVALLNEDDGLVVDAVLCDSDELQFAFSSTLANYHATNPRYHELARLLHELMPKRPLGTQYSCIGFHHLGKVAVMNEILTEHRRSKEKLATAPGFKGTVAIAFTMPCSAYVLKIIRDHPTDDYKFDYFDGLDAVLRKYNLVHEIDRAGSMLDNIIYSNVKLARTMFAPDLLDELLEAGIGTVTLERDALVFRHLIVQIKLTPLPLYLTTAAAADARAAVINLGDCIKNNAAADIFNKDLDGRNYGVSRIRKVYLFDYDAVEQLTEVKVRSTPPMPRAEDEDGVVFRPAQMLEGLRIDDPGLRRAFRDAHPELMQPDYWEGMQHALRAGKVPKVMNYPTSRRLRR

aceK

Isocitrate dehydrogenase kinase/phosphatase

605 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.293 kDa

MTATRHPFASDIDAATRIAEPDFDLLDALVRTDDPDDQAHTLARVVLAAFDNYYAVSRRIPALAQAAFEARDWAATVRLSKIRLGLYTACIDQLVPLLKAGLPELANDEQLWARAEAELLAAIAERYEADFAFAFWQSLRRKLVSDEWRPVSYDTGPAARPKATSAAILKTIATTLPIRPAVIRDILDGAGLRGPWRDRDGDAALAAAAIEAALEPLGPRAGETAKIEIAESGFFRNRGACLVGRVRLRDRGDMPMRNLPLLIALLNEDDGLVVDAVLCDADELQYAFSSTLANYHATNPHYHELARLLHELMPKRPLGTQYSCIGFHHLGKVAVMTEILAEHRRSKEKLDTAPGFKGTVAIAFTMPSSAYVLKIIRDHPTDDYKFDYFDGLDAVLRKYNLVHEIDRAGSMLDNIIYSNVKLERTMFAPDLLDELLESGIDTVTLERGALVFRHLIVQIKLTPLPLYLTTASAADARAAVINLGDCIKNNAAADIFNKDLDGRNYGVSRIRKVYLFDYDAVEPLTDVRVRGDDAPPGPEFEDGVVFRPADMLGGLRIDDPALRRAFRDAHPELMQPEYWQGMQRALRAGKVPRVMNYPAARRLRR

aceK

Isocitrate dehydrogenase kinase/phosphatase

605 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

69.95 kDa

MNHFPKLLSSQIGFDVAQTMLEYFDRHYRIFREAAVDAKTLFERGDWHGLQRLARERITSYDERVKECVEVLEDEYDAENIDDEVWQQIKLHYIGLLTSHRQPECAETFFNSVCCKILHRSYFSNDFIFVRPAISTEYLENDEPAAKPTYRAYYPGTDGLAVTLERIVTNFQLDPPFEDLTRDIGCVMQAIDDEFGHFDEAPNFQIHVLSSLFFRNKSAYIVGRIINADRVLPFAVPIRHVRPGVLALDTVLLRRDLLQIIFSFSHSYFLVDMGVPSAYVDFLCTIMPGKPKAEIYTSVGLQKQGKNLFYRDLLHHLSHSSDRFIIAPGIKGLVMLVFTLPSFPYVFKIIKDHFPPPKETTRAQIMEKYQLVKRHDRLGRMADTLEYSSVALPLARLDHALVRELEKEVPSLLEYEDDKLVIKHLYIERRMTPLNLYLQNGSDADVEHGVKEYGNAVKELMKANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRRVPPPRNEEDELSGEPWYTVGPHDIFPETYGPFLLGDPRVRSVFMKHHADFFDPALWQASKDKLMQGELPDFYPYDATLRFSVRYPARFGATGENDGAGDAQRAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

605 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

69.92 kDa

MNHFPKLLSSQIGFDVAQTMLEYFDRHYRIFREAAVDAKTLFERGDWHGLQRLARERITSYDERVKECVEVLEDEYDAENIDDEVWQQIKLHYIGLLTSHRQPECAETFFNSVCCKILHRSYFSNDFIFVRPAISTEYLENDEPAAKPTYRAYYPGTDGLAVTLERIVTNFQLDPPFEDLTRDIGCVMQAIDDEFGHFDEAPNFQIHVLSSLFFRNKSAYIVGRIINADRVLPFAVPIRHVRPGVLALDTVLLRRDLLQIIFSFSHSYFLVDMGVPSAYVDFLCTIMPGKPKAEIYTSVGLQKQGKNLFYRDLLHHLSHSSDRFIIAPGIKGLVMLVFTLPSFPYVFKIIKDHFPPPKETTRAQIMEKYQLVKRHDRLGRMADTLEYSSVALPLARLDHALVRELEKEVPSLLEYEDDKLVIKHLYIERRMTPLNLYLQNGSDADVEHGVKEYGNAVKELMKANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRRVPPPRNEEDELSGEPWYTVGPHDIFPETYGPFLLGDPRVRSVFMKHHADFFDPALWQASKDKLMQGELPDFYPYDAALRFSVRYPARFGATGENDGAGDAQRAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

605 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

69.95 kDa

MNHFPKLLSSQIGFDVAQTMLEYFDRHYRIFREAAVDAKTLFERGDWHGLQRLARERITSYDERVKECVEVLEDEYDAENIDDEVWQQIKLHYIGLLTSHRQPECAETFFNSVCCKILHRSYFSNDFIFVRPAISTEYLENDEPAAKPTYRAYYPGTDGLAVTLERIVTNFQLDPPFEDLTRDIGCVMQAIDDEFGHFDEAPNFQIHVLSSLFFRNKSAYIVGRIINADRVLPFAVPIRHVRPGVLALDTVLLRRDLLQIIFSFSHSYFLVDMGVPSAYVDFLCTIMPGKPKAEIYTSVGLQKQGKNLFYRDLLHHLSHSSDRFIIAPGIKGLVMLVFTLPSFPYVFKIIKDHFPPPKETTRAQIMEKYQLVKRHDRLGRMADTLEYSSVALPLARLDHALVRELEKEVPSLLEYEDDKLVIKHLYIERRMTPLNLYLQNGSDADVEHGVKEYGNAVKELMKANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRRVPPPRNEEDELSGEPWYTVGPHDIFPETYGPFLLGDPRVRSVFMKHHADFFDPALWQASKDKLMQGELPDFYPYDATLRFSVRYPARFGATGENDGAGDAQRAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

605 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

69.925 kDa

MNHFPKLLSSQIGFDVAQTMLENFDRHYRIFREAAVEAKTLYEHGDWHGLQRLARERITSYDDRVKECVEVLEDEYDAENIDDEVWQQIKLHYIGLLTSHRQPECAETFFNSVCCKILHRSYFSNDFIFVRPAISTEYLENDEPAAKPTYRAYYPGTDGLATTLERIVTNFQLEPAFDDLPRDIGCVMQAIHDEFGHFDEAPNFQIHVLSSLFFRNKSAYIVGRIINADRVLPFAVPIRHVRPGVLSLDTVLLRRDQLMIIFGFSHSYFLVDMGVPSAYVDFLCTIMPGKPKAEIYTSVGLQKQGKNLFYRDLLHHLSHSSDRFIIAPGIKGLVMLVFTLPSFPYVFKIIKDHFPPPKETTRAQIMEKYQLVKRHDRLGRMADTLEYSSVALPIARLDHALVRELEKEVPSLLEYEDGNLVIEHLYIERRMTPLNLYLQNGSDSDVEHGVKEYGNAVKELMKANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRRVPPPRNEEDELSGEPWYTVGPHDIFPETYGPFLLGDPRVRDVFMKHHADFFDPALWQASKDKLIQGELPDFYPYDTALRFCTRYPARFGATDQNDGAGDAQRAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

605 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

70.256 kDa

MNHFPKLLSSQIGFDVAQSMLEYFDRHYRIFREAAVEAKALFERADWHGLQRLARERITSYDERVQECVEVLQDEYDAESIDDEVWQQIKLHYIGLLTSHRQPECAETFFNSVCCKILHRSYFNNDFIFVRPAISTEYLENDEPAAKPTYRAYYPGTDGLAVTLERIVTNFQLEPPFEDLARDIACVMQAIHDEFGRFDEAPNFQIHVLSSLFFRNKSAYIVGRIINADRVLPFAVPIRHVRPGLLALDTVLLRRDLLQIIFSFSHSYFLVDMDVPSAYVDFLCTIMPGKPKAEIYTSVGLQKQGKNLFYRDLLHHLSHSSDRFIVAPGIKGLVMLVFTLPSFPYVFKIIKDHFPPPKETTRRQIMEKYLLVKRHDRLGRMADTLEYSSVALPLARLDHALVRELEKEVPSLLEYEGDNLVIKHLYIERRMTPLNLYLQNGTDAEVEHGVKEYGNAVKELMKANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRRVPPPRNEEDELSGEPWYTVGPHDIFPETYGPFLLGDPRVRAAFLKHHADFFDPALWQASKDKLLQGELPDFFPYDASLRFCVRYPERFRATDERAPARGAQRAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

603 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

69.894 kDa

MNHFPKLLSSQIGFDVAQTILENFDRHYRIFREAAVEAKDLFERADWHGLQRLARERITSYDDRVRECVELLEDEYDAENIDNEVWPQIKLHYIGLLTSHRQPECAETFFNSVCCKILHRAYFNNDFIFVRPAISTEYIENDEPAAKPTYRAYYPGSEGLAATLERIVTNFQLNPPFEDLERDIACIMQAIHDEFGAFDEAVNFQIHVLSSLFYRNKTAYVVGRIINGDRVLPFAVPIRHARAGILALDTVLLRRDQLKIIFSFSHSYFLVDMNVPSAYVQFLRSIMPGKPKAEIYTSVGLQKQGKNLFYRDLLHHLSHSSDRFIVAPGIKGLVMLVFTLPSFPYVFKMIKDHFPPPKDTTREQIMAKYLLVKRHDRLGRMADTLEYSSVALPLARLDDALVRELEKEVPSLIEYEGENLVIKHLYIERRMVPLNLYLQNGSDAEIEHGVREYGNAVKELMQANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRRVPPPRNDEDEMSGEPWYTVGPHDIFPETYAPFLLGDPRVREHFLAHHADFFDPQLWQDSKDRLLRGELPDFFAYEPALRFCIRYPERFAPGDAADGGKLAAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

603 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

69.894 kDa

MNHFPKLLSSQIGFDVAQTILENFDRHYRIFREAAVEAKDLFERADWHGLQRLARERITSYDDRVRECVELLEDEYDAENIDNEVWPQIKLHYIGLLTSHRQPECAETFFNSVCCKILHRAYFNNDFIFVRPAISTEYIENDEPAAKPTYRAYYPGSEGLAATLERIVTNFQLNPPFEDLERDIACIMQAIHDEFGAFDEAVNFQIHVLSSLFYRNKTAYVVGRIINGDRVLPFAVPIRHARAGILALDTVLLRRDQLKIIFSFSHSYFLVDMNVPSAYVQFLRSIMPGKPKAEIYTSVGLQKQGKNLFYRDLLHHLSHSSDRFIVAPGIKGLVMLVFTLPSFPYVFKMIKDHFPPPKDTTREQIMAKYLLVKRHDRLGRMADTLEYSSVALPLARLDDALVRELEKEVPSLIEYEGENLVIKHLYIERRMVPLNLYLQNGSDAEIEHGVREYGNAVKELMQANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRRVPPPRNDEDEMSGEPWYTVGPHDIFPETYAPFLLGDPRVREHFLAHHADFFDPQLWQDSKDRLLRGELPDFFAYEPALRFCIRYPERFAPGDAADGGKLAAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

603 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

69.894 kDa

MNHFPKLLSSQIGFDVAQTILENFDRHYRIFREAAVEAKDLFERADWHGLQRLARERITSYDDRVRECVELLEDEYDAENIDNEVWPQIKLHYIGLLTSHRQPECAETFFNSVCCKILHRAYFNNDFIFVRPAISTEYIENDEPAAKPTYRAYYPGSEGLAATLERIVTNFQLNPPFEDLERDIACIMQAIHDEFGAFDEAVNFQIHVLSSLFYRNKTAYVVGRIINGDRVLPFAVPIRHARAGILALDTVLLRRDQLKIIFSFSHSYFLVDMNVPSAYVQFLRSIMPGKPKAEIYTSVGLQKQGKNLFYRDLLHHLSHSSDRFIVAPGIKGLVMLVFTLPSFPYVFKMIKDHFPPPKDTTREQIMAKYLLVKRHDRLGRMADTLEYSSVALPLARLDDALVRELEKEVPSLIEYEGENLVIKHLYIERRMVPLNLYLQNGSDAEIEHGVREYGNAVKELMQANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRRVPPPRNDEDEMSGEPWYTVGPHDIFPETYAPFLLGDPRVREHFLAHHADFFDPQLWQDSKDRLLRGELPDFFAYEPALRFCIRYPERFAPGDAADGGKLAAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

603 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

69.894 kDa

MNHFPKLLSSQIGFDVAQTILENFDRHYRIFREAAVEAKDLFERADWHGLQRLARERITSYDDRVRECVELLEDEYDAENIDNEVWPQIKLHYIGLLTSHRQPECAETFFNSVCCKILHRAYFNNDFIFVRPAISTEYIENDEPAAKPTYRAYYPGSEGLAATLERIVTNFQLNPPFEDLERDIACIMQAIHDEFGAFDEAVNFQIHVLSSLFYRNKTAYVVGRIINGDRVLPFAVPIRHARAGILALDTVLLRRDQLKIIFSFSHSYFLVDMNVPSAYVQFLRSIMPGKPKAEIYTSVGLQKQGKNLFYRDLLHHLSHSSDRFIVAPGIKGLVMLVFTLPSFPYVFKMIKDHFPPPKDTTREQIMAKYLLVKRHDRLGRMADTLEYSSVALPLARLDDALVRELEKEVPSLIEYEGENLVIKHLYIERRMVPLNLYLQNGSDAEIEHGVREYGNAVKELMQANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRRVPPPRNDEDEMSGEPWYTVGPHDIFPETYAPFLLGDPRVREHFLAHHADFFDPQLWQDSKDRLLRGELPDFFAYEPALRFCIRYPERFAPGDAADGGKLAAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

603 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

69.894 kDa

MNHFPKLLSSQIGFDVAQTILENFDRHYRIFREAAVEAKDLFERADWHGLQRLARERITSYDDRVRECVELLEDEYDAENIDNEVWPQIKLHYIGLLTSHRQPECAETFFNSVCCKILHRAYFNNDFIFVRPAISTEYIENDEPAAKPTYRAYYPGSEGLAATLERIVTNFQLNPPFEDLERDIACIMQAIHDEFGAFDEAVNFQIHVLSSLFYRNKTAYVVGRIINGDRVLPFAVPIRHARAGILALDTVLLRRDQLKIIFSFSHSYFLVDMNVPSAYVQFLRSIMPGKPKAEIYTSVGLQKQGKNLFYRDLLHHLSHSSDRFIVAPGIKGLVMLVFTLPSFPYVFKMIKDHFPPPKDTTREQIMAKYLLVKRHDRLGRMADTLEYSSVALPLARLDDALVRELEKEVPSLIEYEGENLVIKHLYIERRMVPLNLYLQNGSDAEIEHGVREYGNAVKELMQANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRRVPPPRNDEDEMSGEPWYTVGPHDIFPETYAPFLLGDPRVREHFLAHHADFFDPQLWQDSKDRLLRGELPDFFAYEPALRFCIRYPERFAPGDAADGGKLAAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

603 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

69.894 kDa

MNHFPKLLSSQIGFDVAQTILENFDRHYRIFREAAVEAKDLFERADWHGLQRLARERITSYDDRVRECVELLEDEYDAENIDNEVWPQIKLHYIGLLTSHRQPECAETFFNSVCCKILHRAYFNNDFIFVRPAISTEYIENDEPAAKPTYRAYYPGSEGLAATLERIVTNFQLNPPFEDLERDIACIMQAIHDEFGAFDEAVNFQIHVLSSLFYRNKTAYVVGRIINGDRVLPFAVPIRHARAGILALDTVLLRRDQLKIIFSFSHSYFLVDMNVPSAYVQFLRSIMPGKPKAEIYTSVGLQKQGKNLFYRDLLHHLSHSSDRFIVAPGIKGLVMLVFTLPSFPYVFKMIKDHFPPPKDTTREQIMAKYLLVKRHDRLGRMADTLEYSSVALPLARLDDALVRELEKEVPSLIEYEGENLVIKHLYIERRMVPLNLYLQNGSDAEIEHGVREYGNAVKELMQANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRRVPPPRNDEDEMSGEPWYTVGPHDIFPETYAPFLLGDPRVREHFLAHHADFFDPQLWQDSKDRLLRGELPDFFAYEPALRFCIRYPERFAPGDAADGGKLAAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

603 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

70.047 kDa

MNHFPKLLSSQIGFDVAQTILENFDRHYRIFREAAVEAKDLFERSDWHGLQRLARERITSYDDRVRECVELLEDEYDAENIDHDVWPQIKLHYIGLLTSHRQPECAETFFNSVCCKILHRAYFNNDFIFVRPAISTEYIENDEPAAKPTYRAYYPGSEGLAATLERIVTNFQLNPPFEDLERDIACIMQAIHDEFGAFDEAVNFQIHVLSSLFYRNKTAYIVGRIINGDRVLPFAVPIRHARAGVLALDTVLLRRDQLKIIFSFSHSYFLVDMNVPSAYVQFLRSIMPGKPKAEIYTSVGLQKQGKNLFYRDLLHHLSHSSDRFIIAPGIKGLVMLVFTLPSFPYVFKMIKDHFPPPKETTREQIMDKYLLVKRHDRLGRMADTLEYSSVALPLARLDDALVRELEKEVPSLIEYEGDSLVIKHLYIERRMVPLNLYLQNGSDAEIEHGVREYGNAVKELIQANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRRVPPPRNDEDEMSGEPWYTVGPHDIFPETYAPFLLGDPRVREHFLAHHADFFDPQLWQDSKDRLLRGELPDFFAYEPALRFCLRYPERFAPGDAAEDGKRAAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

603 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

69.894 kDa

MNHFPKLLSSQIGFDVAQTILENFDRHYRIFREAAVEAKDLFERADWHGLQRLARERITSYDDRVRECVELLEDEYDAENIDNEVWPQIKLHYIGLLTSHRQPECAETFFNSVCCKILHRAYFNNDFIFVRPAISTEYIENDEPAAKPTYRAYYPGSEGLAATLERIVTNFQLNPPFEDLERDIACIMQAIHDEFGAFDEAVNFQIHVLSSLFYRNKTAYVVGRIINGDRVLPFAVPIRHARAGILALDTVLLRRDQLKIIFSFSHSYFLVDMNVPSAYVQFLRSIMPGKPKAEIYTSVGLQKQGKNLFYRDLLHHLSHSSDRFIVAPGIKGLVMLVFTLPSFPYVFKMIKDHFPPPKDTTREQIMAKYLLVKRHDRLGRMADTLEYSSVALPLARLDDALVRELEKEVPSLIEYEGENLVIKHLYIERRMVPLNLYLQNGSDAEIEHGVREYGNAVKELMQANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRRVPPPRNDEDEMSGEPWYTVGPHDIFPETYAPFLLGDPRVREHFLAHHADFFDPQLWQDSKDRLLRGELPDFFAYEPALRFCIRYPERFAPGDAADGGKLAAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

603 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

69.894 kDa

MNHFPKLLSSQIGFDVAQTILENFDRHYRIFREAAVEAKDLFERADWHGLQRLARERITSYDDRVRECVELLEDEYDAENIDNEVWPQIKLHYIGLLTSHRQPECAETFFNSVCCKILHRAYFNNDFIFVRPAISTEYIENDEPAAKPTYRAYYPGSEGLAATLERIVTNFQLNPPFEDLERDIACIMQAIHDEFGAFDEAVNFQIHVLSSLFYRNKTAYVVGRIINGDRVLPFAVPIRHARAGILALDTVLLRRDQLKIIFSFSHSYFLVDMNVPSAYVQFLRSIMPGKPKAEIYTSVGLQKQGKNLFYRDLLHHLSHSSDRFIVAPGIKGLVMLVFTLPSFPYVFKMIKDHFPPPKDTTREQIMAKYLLVKRHDRLGRMADTLEYSSVALPLARLDDALVRELEKEVPSLIEYEGENLVIKHLYIERRMVPLNLYLQNGSDAEIEHGVREYGNAVKELMQANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRRVPPPRNDEDEMSGEPWYTVGPHDIFPETYAPFLLGDPRVREHFLAHHADFFDPQLWQDSKDRLLRGELPDFFAYEPALRFCIRYPERFAPGDAADGGKLAAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

602 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

69.768 kDa

MNHFPKLLSSQIGFDVAETLLAGFDRHYCIFREAAIRAKNLFEAADWHGLQKLARERITSYDERVRECIAKLEDEYDAENIDDDVWQQIKLHYIGLLTTHRQPECAETFFNSVCCHILHRSYFNNDFIFVRPAISTEYIENDEPAAKPTYRAYYPGKDGLAVTLERIVTNFQLNPPFENLTRDVQCVIQALRDNFGTFNEAPNFQIHVLSSLFFRNKAAYIIGRIINGDMMLPFALPVHHVKPGLLALDALLCKRDQLLIIFSFAHSYFLVDMEVPSAYVEFLGSILHGKPKAEIYTSVGLQKQGKNLFYRDLLRHLKHSSDRFIIAPGIKGMVMLVFTLPSFPYVFKLIKDAFPPPKETTREQVVGKYQLVKRHDRLGRMADTLEYSSVALPLSRLDDALIRELEKEAPSMLEYEGDNLVIRHVYIERRMVPLNIFLQNGTDADIEHGIREYGNAVKELMQANIFPGDMLYKNFGVTRHGRVVFYDYDEIEYLTDCNVRAVPPPRNEEDEMSGEPWYSVGPHDIFPETYNTFLLGDPRVRESFLKHHADFFDPALWQKQKDYILRGELPDFYPYDRSLRFSIRYPERFAADHVTAATERAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

602 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

70.101 kDa

MFPRRLDSPAAYGIAQAMMDGFDRHYRLFRAESARAKHRFETSDWSGQQRAQRERIEFYDLRVKECVRRLEKEFSAGAQPMDVWHQVKLHYIGLLVGHRQPELAETFFNSVTTKILHRTHFHNDFIFVRPAISTEYLENDEPGARPTYRAYYPTPESLQETLVRVVDNFQLQGEFEDLARDAGRVAEVMRPRLGPAKWRANFQIQVLSSLFYRNKGAYLVGKVINGFQELAFALPILHGTDGRYVIDAALFGEDDLQMLFSFARAYFMVDMEIPSAYVQFLRSLMPRKPRAELYNALGLAKQGKTLFYRDFLHHLRYSSDRFRIAPGIKGMVMLVFDLPSFPFVFKVIKDYYPPQKDTTREQIKGKYLLVKQHDRVGRMADTLEYSEVAFPRERFEDDLIAEIEKFAPSQLEISDRDGDGNVEVILKHVYIERRMIPLNIYLQEAFDAGPHDARARQQMERSVVEYGNAIKDLVAANIFPGDMLWKNFGVTRNGKVVFYDYDEIEYLTDCHFRRVPAPRNEEDELSGEVWWAVGPRDVFPETFGPFLLGNDAVREVFMRHHADLLDPVFWQSHKERIQAGHMYDVFPYDPERRFGAGTGSPA

aceK

Isocitrate dehydrogenase kinase/phosphatase

600 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

68.516 kDa

MIYSGDVQRIEPAPVAGPAPLDVAHLILAGFDRHYALFRYSAQRAKSLFESGDWHGMQRLSRERIEYYDMRVRECATQLDSALRGSDARTADGSRANGSAALSEAQTAFWQAVKQEFVGLLADHRQPECAETFFNSVSCRILHRDYFHNDFLFVRPAIATDYLDSRIPSYRVYYPVAEGLHKSLIRMVADFGLAVPYADLPRDAGPRLASDCQIQVLGSLFFRNTGAYIVGRLINQGTVYPFAVALRRNPAGQVCLDALLLGTDDLSTLFSFTRAYFLVDMETPAAVVNFLASLLPRKPKAELYTMLGLQKQGKTLFYRDFLHHLTHSRDAFDIAPGIRGMVMCVFTLPSYPYVFKLIKDRIDKDGMDHATVRRKYQMVKLHDRVGRMADTWEYSQVALPRSRFAPRLLEELRRLVPSLIEENGDTVVIRHVYIERRMMPLNLYLRHASDPLLEVAVREYGDAIRQLATANIFPGDMLYKNFGVTRLGRVVFYDYDEIQRMTEMNFRAIPPAPNEEAELSSEPWYAVGPNDVFPEEFGRFLLGDPRVRQAFLRHHADLLAPQWWQACRARVAQGRIEEFFPYDTDRRLHPQAAPPPRAAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

596 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

69.185 kDa

MPPRGLELLIAQTILQGFDAQYGRFLEITAGAQHRFEQADWHAVQQAMKSRIHLYDHHVGLVVEQLRCIMEGKATDPDFLLRVKRHYTDLLPDYPRFEIAESFFNSVYCRLYDHRSLTPDRLFIFSSQPERRFRTMPRPLAKNFFPEQGWQPLLTTLLTDLPLRLPWQDLARDVRYIIAHLNETLGPARLAQAHLEMANELFYRNKAAWLVGKLRLPDATLPFLLPVHRSDDGELFVDTCLTGSAGASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLHYLRHADEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDRFAPQKEMSEAHVRACYQLVKEHDRVGRMADTQEFENFVIEKRRISPELMALLQQEVGQKLTDMGDKISISHLYIERRMVPLNIWLEQATGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDELSAEPWYSVAPGDVFPEEFRHWLCADPKIGPLFEEMHSDLFSASYWRALQTRIREGYVEDVYAYRRRQRFCVRWKNHNGHPEAAVSAIAPSAVGEG

aceK

Isocitrate dehydrogenase kinase/phosphatase

594 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

68.844 kDa

MTRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKQRIHLYDHHVGLVVEQLRCITEGKSTDVDFLLRVKQQYTQLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERPFRTLPRPLAKDFFPERGWSHLLGKVLSDLPLRLPWQNKARDIGYIIASLQEALGEELLATCHLQVANELFYRNKAAWLVGKLVMPMATLPFLLPIHRSEEGELFVDTCLTTHAEASIVFGFARSYFMVYAPLPGALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLHYITRCDEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDRFAPQKEMTAAHVRACYQLVKEHDRVGRMADTQEFENFVLDKRQIAPALLALLQAEAGNKLTDLGDRIVISHLYIERRMVPLNLWLEQVNGQALRDAVEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFREIPPPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLLRADYWRALQMRIKNGHVEDVYAYRRKQRFSVRYGADSRPDKAFTPPSGKVRRSA

aceK

Isocitrate dehydrogenase kinase/phosphatase

594 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

68.841 kDa

MTRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKQRIHLYDHHVGLVVEQLRCITEGKSTDVDFLLRVKQQYTQLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERPFRTLPRPLAKDFFPERGWSHLLGKVLSDLPLRLAWQNKARDIGYIIASLQEALGEELLATCHLQVANELFYRNKAAWLVGKLVMPMATLPFLLPIHRSDEGELFVDTCLTTHAEASIVFGFARSYFMVYAPLPGALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLHYITRCDEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDRFAPQKEVTAAHVRACYQLVKEHDRVGRMADTQEFENFVLDKRQIAPGLLALLQAEAGNKLTDLGDRIVISHLYIERRMVPLNLWLEQVNGQALRDAVEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRQIPPPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLLRADYWRELQTRIKNGHVEDVYAYRRKQRFSVRYGADSRPDKVFTPPSGRVRRSA

aceK

Isocitrate dehydrogenase kinase/phosphatase

593 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

69.788 kDa

MKISVGLYGTNAHQIALAMIQGFNKHYTLFRQTSREAKTRFEQADWLGVHKAVKERIRFYDDRVDECVERLRNQFDAASIDDTTWQQVKLLYIGLLLNHKQPELAETFFNSVTTKILHRNYFHNDFIFVRPSISTENIEGDDTQTYRSYYAKEDGLRGTVLKIVKDFDWHRPFVDLEHDVEHVYHAVRHFLNGMPPREVNFQIQVLGSAFYRNKAAYIIGKAINGATEYPFTIPVLQNEAGQLYLDTILLDAWRIGLLFSLSRAYFMVDMEVPSGYVQFLRSILPAKPRSELYIMLGLGKQGKTMFFRDLIYHLHHSEDKFIMAPGIRGLVMLVFTLPSYPYVFKLIKDVFGSSKEMDRATVKKKFMMVKQVDRVGRMADTLEFSNVMFPLKRFNDEVLAELQQLAPSCFEVDGDQLIIKHLYIERRMEPLNIHLDRMERANNVERLEHVIREYGSAIREMAQANIFPGDMLWKNFGVTRFGRVVFYDYDEIEYMTDIKFRQIPPAPDFETEMSGEVWYAVSRNDVFPEEFATFLLTSPQVRKIFIKYHKDLLSPRFWLEAQEKIRSGYVEDFFPYPQELRFINRQTDLTEEQ

aceK

Isocitrate dehydrogenase kinase/phosphatase

593 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

69.249 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKSRIHLYDHHVGLVVEQLRCITDGKSTDADFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFFPDHGWEPLLMRILSDLPLCLPWQNKSRDIRYIIAHLTETLGEDALPRCHVQVANELFYRNKAAWLVGKLTTPDGTLPFLLPIHRTDEGELFVDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLCYLAESDEKFIEAPGIRGMVMLVFTLPGFDRVFKIIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLDKRQIDPALMALLRQEAPEKITDLGEHIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPARYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQTRIKEGHVEDVYAYRRRQRFSVRYETDRRPDKAFAPPSGNVRRA

aceK

Isocitrate dehydrogenase kinase/phosphatase

591 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

69.173 kDa

MTRDLEKLVAQTILQGFDAQYGRFLEVTAGAQQRFEQADWPAVQQAMKQRIHLYDHHVGLVVAQLRCITGIRCDDADFLARMKHIYTGLLPDYPRFEIAESFFNSVYCRLFNHRELAPDKLFVFSSQPEKRFHEIPRPIAKTFVPTDGWQRMLEKLLGDVPLRLPWEDLPRDIDYIVTYLQSTFSAEQLEQATLQVANELFYRNKAAWLAGKLSLPDGVFPFLLPIHHNERGALFIDTCLTAQADASMVFGFARSYFMVYAPQPSALVAWLRDILPGKTTAELYLAIGCQKHSKTEYYREYLHYIAESEEQFIIAPGVKGMVMLVFTLPSFDRVFKVIKDRFAPQKEVSAERVMACYQLVKEHDRVGRMADTQEYENFVIDKHRISPELLDELWREVPEKLEDLGDQLVIRHLYMERRMTPLNLYLEQANAQQLHDVIEEYGNAIKQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRKIPPPRYLEDELAAEPWYSVAPNDVFPEEFPHFLCSDRHIRTLFEEMHGDLFCADYWRALQQRIREGHIEDVYAYRRRKRFSQRAEPLYITTENDSGLCRYPA

aceK

Isocitrate dehydrogenase kinase/phosphatase

591 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

69.249 kDa

MTRDLEKLVAQTILQGFDAQYGRFLEVTAGAQQRFEQADWPAVQQAMKQRIHLYDHHVGLVVEQLRCITGIRCDDADFLARVKHIYTRLLPDYPRFEIAESFFNSVYCRLFNHRELTPDKLFVFSSQPEQRFREIPRPIAKTFVPTDGWQNMLEKLLSDVPLRLPWEDLPRDIGYIVAYLQRTFSAEQLAQATLQMANELFYRNKAAWLVGKLSLPDGIFPFLLPIHHNERGALFIDTCLTSQADASIVFGFARSYFMVYAPLPSALVAWLRDILPGKTTAELYLAIGCQKHSKTEYYREYLHYIAESEEQFIIAPGVKGMVMLVFTLPSFDRVFKVIKDRFAPQKEVSAERVMACYQLVKEHDRVGRMADTQEYENFVIDKHRISSELLDELWREVPDKLEDLGDRLVIRHLYMERRMTPLNLYLEQANAQQLHDVIEEYGNAIKQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRKIPPPRHPEDELAAEPWYSVAPNDVFPEEFPHFLCSDRHIRTLFEEMHGDLFCADYWRALQQRIREGHIEDVYAYRRRKRFSQRADPRYTTAENDSGFCRNPA

aceK

Isocitrate dehydrogenase kinase/phosphatase

591 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

69.162 kDa

MDASVGENPVAQSIAQAMIEGFNKHYRIFRETSRRAKESFEAAEWQAQIDAVRERVQFYDERVDEAVRRLHEEFDADSLDDSTWQQLKLQYIGILMRHKQPELAETFFNSVCCKILHRTYFNNDYLFARPAVSTEYIESYPPVYSSYYPQDEGLRTTVRRIIEDFDWQRPFANLDRDIDNILRAVHEHIGAWPDMEVNCQIQVLYSAFYRNKTAYIIGKAINGYQEYPFALAVRHNPAGRLEADTILLDPWRISVLFSLSRAYFLVDMEVPSGYVHFLRSIMPNKHRSELYTMLGLGKQGKTMFFRDLIAHLRHSNDQFIIAPGIRGLVMLVFTLPSYPYVFKIIKDVFGASKNMDRATVKRKYLMVKQVDRVGRLADTLEFSYAALPLSRFHPELLDELRALAPSSFEIEGDSVIIKHLYIERRMTPLNIYLEHADDDQVEYAVREYGNAIRELATANIFPGDMLWKNFGVTRYGRVVFYDYDEIEFMTAMNFRRIPPAPYPEMEMAAEPWYSAGPMDVFPEEFATFLLGAPRVRKAFLKHHRDLLDAKFWQDVQASIRKGYLEDFFPYPTELRFCNMWSNERGRAHQAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

589 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

68.578 kDa

MKDELALTIANTIINGFERHFAIFTEITQSARNRFQQCQWNEIHRSARARTNFYDERVKETFNDIKEDFNISSLDDALWQRVKAVYSDLLINHKQPELAETFYNSVFCHLFERKYYHNDYIYVESTAHRLDDKTQPEIYTSYQPKELGLKQTICDIMNSHRTVIPFEDLDRDVDALINTFRRKAHKTRVKLEDLKFDILNFTFYRNKGAYLIGRVLSPAGETPFIIAVLNNEKGGLYIDALLTSSESMAVVFGFARAYFFVDCEHPYALVNFLQGLMPHKTKADLYSAIGFHKQGKTQFYRDFLNHLDSSDDQFELAAGIKGMVMSVFTLPSYPYVFKIIKDKFSPSKNITKKDVKGKYRLVKLHDRVGRMADTMEYSEVAFPKSRFNDELLAELQKVAPSIIRYEGEGEEALIIIEHLYIERRMVPLNLYLMDALKNKAQQKIDDALFGYGQAIKQLISADIFPGDMLLKNFGVTRHGRVIFYDYDEIAYMNEINFRVKPKAVTEEQLYAAEPWYSVMPGDMFPEELATFALANPSYLKAFKIHHEDLLTAAYWQQCQQDVANGIYKDVFPYPDKYRFCNLSFGSIKR

aceK

Isocitrate dehydrogenase kinase/phosphatase

589 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

68.168 kDa

MDAQVGDNPVAQAIAHALVEGFNKHYRIFRGTSRRAKEYFEAGDWRAQLDAVRDRVQFYDDRVDETVRRLLEEFDADSLDDATWQQVKLHFIGALINHKQPELAETFFNSVGCKILHRTYFNNDYIFARPAISTEYIESYPPVYSSYYPQDGGLRATIRRIIEDFDWQRPFEDLDRDIDCIMRAALAHLGEWPAMEVNCQLQVLYSAFYRNKTAYIIGKVINGWQDYPFTLAVRHGASGRLVIDTILLDPWRISVLFSLSRAYFMVDMEVPSGYVQFLRSIMPNKPRSELYTMLGLGKQGKTMFFRDLVAHLRHSNDQFIIAPGIRGLVMLVFTLPSYPYVFKIIKDVFGSSKNMDRATVKRKYLMVKQVDRVGRMADTLEFSYAALPLSRFHPELLEELRTLAPSAFEIDGDALVLKHFYIERRMTPLNIHLEKASDGEVEAAVHEYGNAIRELAIANIFPGDMLWKNFGVTRYGRVVFYDYDEIEYMTSMNFRRIPPAPHEDMELSGEPWYSAGPMDVFPEEFATFLLGSPRVRKAFMKYHRDLLEPAFWQAAQQGVRDGHVEDFFPYPAELRFSVMFPATPVAAQD

aceK

Isocitrate dehydrogenase kinase/phosphatase

586 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

65.597 kDa

MLDERGALARGAAEAIRAGYEAYQAERARITARARGRFEARDWAGAQRDARERLDLRDGVVHRTVGEVRAELGGAVQDREVWRRAKEAFEAVAAARPDAEIAGSFFNSVTRRVLTTVGVDPAIEFLAADAPPPREDPPQHRAFAREATTEALLARILRAAPISAPFEDLARDARLAALELDAHVRGLPDRQPIDAVELARPVFYRGKGAYLVGRIRRGRHLTPLVLALAHGDRGVALDAVLFTEEDVSIVFGFTRSYFHVALERPRAMVAFLSTLLPLKRRSELYTGLGYHKHGKAELYREVAQHLAEGDDRFVPARGDRGLVMCVFTLPGLDVIFKVIRDRFAPPKQTTRREVMDRYRHVFRHDRAGRLVDAQEYEHLAFPAARFSPALLEELRTECGDGVRVAGGEVAIRHLYAERRVTPLNLFVREADEWTARQAVLDFGCALRDLAATDTFPGDLLLKNFGVTRHGRVIFYDYDELTRVTDCNFRDLPGAGPGDGDDGWGGGPDAGYDGGDPPFYVGPADVFPEELLPFLGLTGRLREVFLRAHGELLTGRWWRDIQARLRAGEIVDIFPYREEQRLRHAHP

aceK

Isocitrate dehydrogenase kinase/phosphatase

585 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

68.791 kDa

MGIDSAHLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKKRINLYDHHVGLVVEQLKCIHSAFGYDEEYIAKVKVVYTGLLPDYPRFEIAESFFNSVYCRLFEHRNLTPDKLFIFTSQPARRFRDIPRPLSRDFFPNDNLALMLRTILNDLPLRLPWENLERDIYYITDYLQQTFPVGELLQATFQIANELFYRNKAAWLVGKIRIGGQVYPFLLPIHHNESGGIFIDTCLTDYADASIVFGFARSYFMVYAPLPAALVEWLREILPAKSTSELYMAIGCQKHGKTEYYREYLAFITFSKEQLIIAPGVKGMVMLVFTSPSFDRVFKVIKDQFAPQKEVTQERVQECYRLVKEHDRVGRMADTQEFENFVIDKARISPELMEELQKEVPEKLEDLGDKILIKHLYMERRMTPLNIYMEQVEERKLKDVIEEYGNAIKQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDELAGEPWYSVAPNDVFPEEFRHFLCTDSRIRRYFEEMHSDLFKADYWRALQERIRSGHVEDVFAYRRKQRFSQRTEIETYSIAKVSA

aceK

Isocitrate dehydrogenase kinase/phosphatase

584 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.747 kDa

MAAKLELLIAQTILQGFDAQYGRFLEVTAGAQQRFERADWPAVQQAMKKRIHLYDHHVGLVVEQLKCITGQQYFDADFPSRVKAVYTDLLPEYPRFEIAESFFNSVYCRLFRHRDLTPEKLFVFSSQPEGRFRDIPRPLSRDFTANGDVSAMLYNLLTDLPLRLPWENLSRDIDYITLALQQSFSAQQLAGATFQIANELFYRNKAAWLVGKLRVADRVYPFLLPIHHSDSGALFIDTCLTSKAEASIVFGFARSYFMVYAPLPAAMVEWLREILPGKTTAELYMAIGCQKHGKTECYREYLTFMSGSQEQFIIAPGVKGMVMLVFTLPSFDRVFKVIKDEFAPQKEVTQAQVMACYQLVKEHDRVGRMADTQEYENFVVDKARLSPELLAELQREVPDKLEDLGDRIAIRHLYMERRMTPLNLYLEQADEQQMRDAIEEYGNAIKQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDELASEPWYSVSPNDVFPEEFRHFLCGDRRIRQVFEEMHRDLFEADYWRGLQQRIRDGHVEDVFAYRKKRRFSQRSGAALPATSATA

aceK

Isocitrate dehydrogenase kinase/phosphatase

583 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.956 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKSRIHLYDHHVGLVVEQLRCITDGKSTDADFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFFPDHGWEPLLMRILSDLPLRLPWQNKSRDIRYIIAHLTETLGEDALPRCHVQVANELFYRNKAAWLVGKLTTPDGTLPFLLPIHRTDEGELFVDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLCYLAESDEKFIEAPGIRGMVMLVFTLPGFDRVFKIIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLDKRQIDPALMALLRQEAPEKITDLGEHIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPARYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQTRIKEGHVEDVYAYRRRQRFSVRYGAISSTANSS

aceK

Isocitrate dehydrogenase kinase/phosphatase

583 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.96 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKSRIHLYDHHVGLVVEQLRCITDGKSTDADFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFFPDHGWETLLMRILSDLPLRLPWQNKSRDIRYIIAHLTETLGEDALPRCHVQVANELFYRNKAAWLVGKLTTPDGTLPFLLPIHRTDEGELFVDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLCYLAESDEKFIEAPGIRGMVMLVFTLPGFDRVFKIIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLDKRQIDPALMALLRQEAPEKITDLGEHIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPARYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQTRIKEGHVEDVYAYRRRQRFSVRYGAISSTANSS

aceK

Isocitrate dehydrogenase kinase/phosphatase

583 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.907 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKSRIHLYDHHVGLVVEQLRCITDGKSTDADFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFFPDHGWETLLMRILSDLPLRLPWQNKSRDIRYIIAHLTETLGEDALPCCHVQVANELFYRNKAAWLVGKLTTPDGTLPFLLPIHRTDEGELFVDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLCYLAESDEKFIEAPGIRGMVMLVFTLPGFDRVFKIIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLDKRQIDPALMALLRQEAPEKITDLGEHIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPARYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQTRIKEGHVEDVYAYRRRQRFSVRYGAISSTANSS

aceK

Isocitrate dehydrogenase kinase/phosphatase

583 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.984 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKSRIHLYDHHVGLVVEQLRCITDGKSTDADFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFFPDHGWEPLLMRILSDLPLRLPWQNKSRDIRYIIAHLTETLGEDALPRCHVQVANELFYRNKAAWLVGKLTTPDGTLPFLLPIHRTDEGELFVDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLCYLAESDEKFIEAPGIRGMVMLVFTLPGFDRVFKIIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLDKRQIDPALMALLRQEVPEKITDLGEHIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPARYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQTRIKEGHVEDVYAYRRRQRFSVRYGAISSTANSS

aceK

Isocitrate dehydrogenase kinase/phosphatase

583 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

68 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKSRIHLYDHHVGLVVEQLRCITDGKSTDADFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFFPDHGWEPLLMRILSDLPLRLPWQNKSRDIRYIIAHLTETLGEDALPRCHVQVANELFYRNKAAWLVGKLTTPDGTLPFLLPIHRTDEGELFVDTCLTTTAEASIVFGFARSYFMVYAPLLAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLCYLAESDEKFIEAPGIRGMVMLVFTLPGFDRVFKIIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLDKRQIDPALMALLRQEVPEKITDLGEHIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPARYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQTRIKEGHVEDVYAYRRRQRFSVRYGAISSTANSS

aceK

Isocitrate dehydrogenase kinase/phosphatase

583 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

68.036 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKSRIHLYDHHVGLVVEQLRCITDGKSTDADFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFFPDHGWETLLMRMLSDLPLRLPWQNKSRDIRYIIAHLTETLGEDALPRCHVQVANELFYRNKAAWLVGKLTTPDGTLPFLLPIHRTDEGELFVDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLCYLTESDEKFIEAPGIRGMVMLVFTLPGFDRVFKIIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLDKRQIDPALMALLRQEVPEKITDLGEHIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPARYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQTRIKEGHVEDVYAYRRRQRFSVRYGAISSTANSS

aceK

Isocitrate dehydrogenase kinase/phosphatase

583 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.956 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKSRIHLYDHHVGLVVEQLRCITDGKSTDADFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFFPDHGWEPLLMRILSDLPLRLPWQNKSRDIRYIIAHLTETLGEDALPRCHVQVANELFYRNKAAWLVGKLTTPDGTLPFLLPIHRTDEGELFVDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLCYLAESDEKFIEAPGIRGMVMLVFTLPGFDRVFKIIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLDKRQIDPALMALLRQEAPEKITDLGEHIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPARYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQTRIKEGHVEDVYAYRRRQRFSVRYGAISSTANSS

aceK

Isocitrate dehydrogenase kinase/phosphatase

583 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

68 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKSRIHLYDHHVGLVVEQLRCITDGKSTDADFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFFPDHGWELLLMRILSDLPLRLPWQNKSRDIRYIIAHLTETLGEDALPRCHVQVANELFYRNKAAWLVGKLTTPDGTLPFLLPIHRTDEGELFVDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLCYLAESDEKFIEAPGIRGMVMLVFTLPGFDRVFKIIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLDKRQIDPALMALLRQEVPEKITDLGEHIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPARYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQTRIKEGHVEDVYAYRRRQRFSVRYGAISSTANSS

aceK

Isocitrate dehydrogenase kinase/phosphatase

583 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.96 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKSRIHLYDHHVGLVVEQLRCITDGKSTDADFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFFPDHGWETLLMRILSDLPLRLPWQNKSRDIRYIIAHLTETLGEDALPRCHVQVANELFYRNKAAWLVGKLTTPDGTLPFLLPIHRTDEGELFVDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLCYLAESDEKFIEAPGIRGMVMLVFTLPGFDRVFKIIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLDKRQIDPALMALLRQEAPEKITDLGEHIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPARYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQTRIKEGHVEDVYAYRRRQRFSVRYGAISSTANSS

aceK

Isocitrate dehydrogenase kinase/phosphatase

583 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.956 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKSRIHLYDHHVGLVVEQLRCITDGKSTDADFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFFPDHGWEPLLMRILSDLPLRLPWQNKSRDIRYIIAHLTETLGEDALPRCHVQVANELFYRNKAAWLVGKLTTPDGTLPFLLPIHRTDEGELFVDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLCYLAESDEKFIEAPGIRGMVMLVFTLPGFDRVFKIIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLDKRQIDPALMALLRQEAPEKITDLGEHIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPARYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQTRIKEGHVEDVYAYRRRQRFSVRYGAISSTANSS

aceK

Isocitrate dehydrogenase kinase/phosphatase

583 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.956 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKSRIHLYDHHVGLVVEQLRCITDGKSTDADFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFFPDHGWEPLLMRILSDLPLRLPWQNKSRDIRYIIAHLTETLGEDALPRCHVQVANELFYRNKAAWLVGKLTTPDGTLPFLLPIHRTDEGELFVDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLCYLAESDEKFIEAPGIRGMVMLVFTLPGFDRVFKIIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLDKRQIDPALMALLRQEAPEKITDLGEHIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPARYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQTRIKEGHVEDVYAYRRRQRFSVRYGAISSTANSS

aceK

Isocitrate dehydrogenase kinase/phosphatase

579 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

66.728 kDa

MNHPSLPPQSERRALAIAQAVYEAFEDYHARFSEITACAKQRFETRDWSGAREDAVARIALYDQYIAECMLRLRAVLLGQAHDRALWMRARDRYAALLSGLIDQELYKTFYNTLTRRYFGTHGVDADIEFIALDIEPTDAITVPVARHTYAVSPGRLTDMLVRVLGDYAFAVPYAHRTRCAAAIAVRLLDDLAHWGEHPVRSVELLETVFYRERRAYLVGRVFGEHRFSPCVIALINDDAGLRAEAVLTRRSDVAQLFSNSRSYFQADLSTVGDAVVFLRSLLTHKPVDELYTMLGRAKQGKTERYRTFFSHFQAHPSEQLVHADGTPGMVMVVFTLPSYPLVFKLIRDRFAYPKTMSRAQVEGKYELVFQLDRIGRLLDAQPYRFLRFPKARFSPALLQELQTSCAMSLSEDGDDVLIALCYVQRRLRPLNLYLREQLPEAAHAAALDYGQAIKDMARNNIFPGDMLLKNFGITRHQRAVFYDYDELCLITECNFRDWPTPATYEEQMAAEPWFHVGPRDVFPERFALFMGLPSSQLEAVKHQHPELFDPRWWRDLQSRLRDDDYPDTPPYAESRRLA

aceK

Isocitrate dehydrogenase kinase/phosphatase

579 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

66.815 kDa

MSHPPLPPQSERRALAIAQAVYEAFEDYHARFSEITARAKQRFETRDWSGAREDAVARIALYDQYIAECMLRLRAVLLGQAHDRALWMRARDHYAALLSGLIDQELYKTFYNTLTRRYFGTHGVDADIEFIALDIEPTDAITVPVARHTYAVSPGRLTDMLVRVLGDYAFAVPYTHRTRCAAAIAVRLLDDLAHWGEHPVRSVELLETVFYRERRAYLVGRVFGEHRFSPCVIALINDEAGLRAEAVLTRRSDVAQLFSNSRSYFQADLSTVGDAVVFLRSLLTHKPVDELYTMLGRAKQGKTERYRTFFSHFQAHPSEQLVHADGTPGMVMVVFTLPSYPLVFKLIRDRFAYPKTMSRAQVEGKYELVFQLDRIGRLLDAQPYRFLRFPKARFSPALLQELQTSCAMSLSEDGDDVLIALCYVQRRLRPLNLYLREQLPEAAHAAALDYGQAIKDMARNNIFPGDMLLKNFGITRHQRAVFYDYDELCLITECNFRDWPVPTTYEEQMAAEPWFHVGPRDVFPERFALFMGLPASQLEAVKHQHPELFDPRWWRDLQSRLREDDYPDTPPYAESRRLA

aceK

Isocitrate dehydrogenase kinase/phosphatase

579 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

66.976 kDa

MNQQPLPPQSERRALAIGRAVYEAFQDYHAQFSQITARARQRFETRDWSGAREDAVARIALYDHYISECMLRLRAVLLGQAHDRALWMRARTHYAELLTGLIDQELYKTFYNTLTRRYFRTQGVDAQIEFIALDIEPTDAITVPVARHTYAVSPGRLTEMLVRVLGDYPFEVPYAHRTRCAAAIAVRLLDDLAHWGEHPVRSVELLETVFYRERRAYLVGRLFGEHRFSPCVIALVNDDAGLRAEAVLTRRSDVAQLFSNSRSYFQADLTTVGDAVVFLRSLLTHKPIDELYTMLGRAKQGKTERYRTFFRHFQAHPAEQLVHADGTPGMVMVVFTLPSYPLVFKLIRDRFAYPKTMSRAQVEGKYELVFQLDRIGRLLDAQPYRFLRFPKARFSPALLQDLQSSCAMSLSEDGDDVLIALCYVQRRLRPLNLYLREQLPAAAHAAALDYGQAIKDMARNNIFPGDMLLKNFGITRHQRAVFYDYDELCLITECTFRDWPTPTSYEEQMAAEPWFHVGPRDVFPERFALFMGLPSSQLEAVKHMHPELFDPQWWRDLQARLREDDYPDTPPYADAQKLA

aceK

Isocitrate dehydrogenase kinase/phosphatase

579 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

66.976 kDa

MNQQPLPPQSERRALAIGRAVYEAFQDYHAQFSQITARARQRFETRDWSGAREDAVARIALYDHYISECMLRLRAVLLGQAHDRALWMRARTHYAELLTGLIDQELYKTFYNTLTRRYFRTQGVDAQIEFIALDIEPTDAITVPVARHTYAVSPGRLTEMLVRVLGDYPFEVPYAHRTRCAAAIAVRLLDDLAHWGEHPVRSVELLETVFYRERRAYLVGRLFGEHRFSPCVIALVNDDAGLRAEAVLTRRSDVAQLFSNSRSYFQADLTTVGDAVVFLRSLLTHKPIDELYTMLGRAKQGKTERYRTFFRHFQAHPAEQLVHADGTPGMVMVVFTLPSYPLVFKLIRDRFAYPKTMSRAQVEGKYELVFQLDRIGRLLDAQPYRFLRFPKARFSPALLQDLQSSCAMSLSEDGDDVLIALCYVQRRLRPLNLYLREQLPAAAHAAALDYGQAIKDMARNNIFPGDMLLKNFGITRHQRAVFYDYDELCLITECTFRDWPTPTSYEEQMAAEPWFHVGPRDVFPERFALFMGLPSSQLEAVKHMHPELFDPQWWRDLQARLREDDYPDTPPYADAQKLA

aceK

Isocitrate dehydrogenase kinase/phosphatase

579 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

66.976 kDa

MNQQPLPPQSERRALAIGRAVYEAFQDYHAQFSQITARARQRFETRDWSGAREDAVARIALYDHYISECMLRLRAVLLGQAHDRALWMRARTHYAELLTGLIDQELYKTFYNTLTRRYFRTQGVDAQIEFIALDIEPTDAITVPVARHTYAVSPGRLTEMLVRVLGDYPFEVPYAHRTRCAAAIAVRLLDDLAHWGEHPVRSVELLETVFYRERRAYLVGRLFGEHRFSPCVIALVNDDAGLRAEAVLTRRSDVAQLFSNSRSYFQADLTTVGDAVVFLRSLLTHKPIDELYTMLGRAKQGKTERYRTFFRHFQAHPAEQLVHADGTPGMVMVVFTLPSYPLVFKLIRDRFAYPKTMSRAQVEGKYELVFQLDRIGRLLDAQPYRFLRFPKARFSPALLQDLQSSCAMSLSEDGDDVLIALCYVQRRLRPLNLYLREQLPAAAHAAALDYGQAIKDMARNNIFPGDMLLKNFGITRHQRAVFYDYDELCLITECTFRDWPTPTSYEEQMAAEPWFHVGPRDVFPERFALFMGLPSSQLEAVKHMHPELFDPQWWRDLQARLREDDYPDTPPYADAQKLA

aceK

Isocitrate dehydrogenase kinase/phosphatase

578 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.671 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFHPDHGWESLLMRVISDLPLRLRWQNKSRDIHYIIRHLTETLGTDNLAESHLQVANELFYRNKAAWLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPALMELLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFSVRYGEMLF

aceK

Isocitrate dehydrogenase kinase/phosphatase

578 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.671 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFHPDHGWESLLMRVISDLPLRLRWQNKSRDIHYIIRHLTETLGTDNLAESHLQVANELFYRNKAAWLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPALMELLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFSVRYGEMLF

aceK

Isocitrate dehydrogenase kinase/phosphatase

578 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.735 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAEFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFHPDHGWESLLMRVISDLPLRLHWQNKSRDIHYIIRHLTETLGPENLSKSHLQVANELFYRNKAAWLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPALMELLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFSVRYGEMLF

aceK

Isocitrate dehydrogenase kinase/phosphatase

578 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.735 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAEFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFHPDHGWESLLMRVISDLPLRLHWQNKSRDIHYIIRHLTETLGPENLSKSHLQVANELFYRNKAAWLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPALMELLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFSVRYGEMLF

aceK

Isocitrate dehydrogenase kinase/phosphatase

578 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.671 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFHPDHGWESLLMRVISDLPLRLRWQNKSRDIHYIIRHLTETLGTDNLAESHLQVANELFYRNKAAWLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPALMELLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFSVRYGEMLF

aceK

Isocitrate dehydrogenase kinase/phosphatase

578 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.699 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFHPDHGWESLLMRVISDLPLRLRWQNKSRDIHYIIRHLTETLGTDNLAESHLQVANELFYRNKAAWLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDRFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPALMELLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFSVRYGEMLF

aceK

Isocitrate dehydrogenase kinase/phosphatase

578 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.699 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFHPDHGWESLLMRVISDLPLRLRWQNKSRDIHYIIRHLTETLGTDNLAESHLQVANELFYRNKAAWLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDRFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPALMELLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFSVRYGEMLF

aceK

Isocitrate dehydrogenase kinase/phosphatase

578 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.671 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFHPDHGWESLLMRVISDLPLRLRWQNKSRDIHYIIRHLTETLGTDNLAESHLQVANELFYRNKAAWLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPALMELLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFSVRYGEMLF

aceK

Isocitrate dehydrogenase kinase/phosphatase

578 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.661 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFHPDHGWESLLMRVISDLPLRLRWQNKSRDIHYIIRHLTETLGTDNLAESHLQVANELFYRNKAAWLVGKLITSSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPALMELLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFSVRYGEMLF

aceK

Isocitrate dehydrogenase kinase/phosphatase

578 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.699 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFHPDHGWESLLMRVISDLPLRLRWQNKSRDIHYIIRHLTETLGTDNLAESHLQVANELFYRNKAAWLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDRFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPALMELLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFSVRYGEMLF

aceK

Isocitrate dehydrogenase kinase/phosphatase

578 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.584 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFHPDHGWESLLMRVISDLPLRLRWQNKSRDIHYIVRHLTETLGTDNLAESHLQVANELFYRNKAAWLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPALMALLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIRDGHVEDVYAYRRRQRFSVRYGEMLF

aceK

Isocitrate dehydrogenase kinase/phosphatase

578 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.671 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFHPDHGWESLLMRVISDLPLRLRWQNKSRDIHYIIRHLTETLGTDNLAESHLQVANELFYRNKAAWLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPALMELLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFSVRYGEMLF

aceK

Isocitrate dehydrogenase kinase/phosphatase

578 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.586 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQLAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERSFRTIPRPLAKDFHPDHGWESLLMRVISDLPLRLRWQNKSRDIHYIIRHLTETLGTDNLAESHLQVANELFYRNKAAWLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPALMELLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFSVRYGEMLF

aceK

Isocitrate dehydrogenase kinase/phosphatase

578 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.712 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAEFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFYPEHGWEALLMRVLSDLPLRLPWQNKSRDINYIIRHLTETLGPENLSESHLQVANELFYRNKAAWLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDRFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPALMELLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRTDYWRALQNRIREGHVEDVYAYRRRQRFSVLYGEMLF

aceK

Isocitrate dehydrogenase kinase/phosphatase

577 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.321 kDa

MNNTHSSVLNKVAYLILHGFDKSYRWHSRITRDAQQRFEQALWQETQKAVKERIAIYERTLADAVGEIYQQVFPHQENNQFWFDLKTRYQKILSDHPQYELAETFYNSVLGRIFKHQKINDEMMFIMPTRCYLAGLQRHLVVHSFDTSGTVRRMLEDIFSQYHFDIAFQDMQRDLQHLDGALRARLNREQLASVHTVEMLKPVFYRSKSAYLIGRICMPDETLPFVIPLSIAEAETSGEKHKIVVEALLTERQDLSVVFSFARAYFMADTQHPAEVVAFLHELLPHKKKFELYIALGLYKHGKTVFYRNFLAHLEESNDQFSIAPGIRGLVMAVFHLPSYGVVFKIIKDEFPESKKITRQHVKDCYKLVKMTDRVGRMADTHEYVNFRLPRHRVEQALVDELLDCCASSIELTDEEVIIKHLYIERKMTPLNIFLEQQPDPALITSALNDLGLCIKQIAAAHIFAGDMLHKNFGITRGGRVIFYDYDEICYLTEREFRTLPKSDDPYAIDTLSVGPTDVFPEQFEHFIVGKKHLKQELKALHGEIMTAEYWQHMQAQSLKGDVPDFIPYNQAKRFVN

aceK

Isocitrate dehydrogenase kinase/phosphatase

577 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

66.698 kDa

MVQSAPASEIAALILRGFDAYREQFREITDGARARFEQAQWQEAQRASAQRINLYEEKVAETVAGLRAGLADSELLDVERWPIIKSAYIAQIDLRLDDELAETWFNSIFCGLFSHDNISDGTMFVHTTRPSLRAHARAPYTRTYRPGGDLRQALEKIFDDYRFDVPYDDRERDLERIDALLHSNLPDWVCKDPDLAIELIGSVFYRNKGAYLVGRLFTPDEQWPLVFPLLHREGHGIQFDTVITDEAEVSIIFSFTRSYFMVDVPVPAELVAFLKRLLPGKHLAELYTSIGFYKQGKSEFYRALINHLATTDDRFVMAPGVRGMVMSVFTLPGFNTVFKIIKDRFNPSKSVDHATVIQKYQLVKNHDRVGRLADTQQFADFRFPVSKFEPECLAELLEVAPSTVVVEGDVVLIRHCWTERRMTPLNIYLENASEAQTREALNDYGLAIKQLAAANIFPGDMLLKNFGVTRHGRVVFYDYDEICYLTEVNFRYIPEPRFPEDEMSSEPWYSVGPNDVFPEEFPRFLFVDLDQRRLFAKLHGNLYDAKYWQGLQQQIREGKVIDVFPYRRQETPEQLLK

aceK

Isocitrate dehydrogenase kinase/phosphatase

577 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

66.774 kDa

MVQSAPASEIAALILRGFDDYREQFREITDGARARFEQAQWQEAQRASAQRINLYEEKVAETVAGLRAGLADSELLDVERWPIIKSAYIAQIDLRLDDELAETWFNSIFCGLFSHDNISDGTMFVHTTRPSLRAHARAPYTRTYRPGGDLRQALEKIFDDYRFDVPYDDRERDLERIDALLHSNLPDWVCKDPDLAIELIGSVFYRNKGAYLVGRLFTPDEQWPLVFPLLHREGHGIQFDTVITDEAEVSIIFSFTRSYFMVDVPVPAELVAFLKRLLPGKHLAELYTSIGFYKQGKSEFYRALINHLATTDDRFVMAPGVRGMVMSVFTLPGFNTVFKIIKDRFNPSKSVDHATVIQKYQLVKNHDRVGRLADTQQFADFRFPVSKFEPECLAELLEVAPSTVVMEGDVVLIRHCWTERRMTPLNIYLENASEAQTREALNDYGLAIKQLAAANIFPGDMLLKNFGVTRHGRVVFYDYDEICYLTEVNFRYIPEPRFPEDEMSSEPWYSVGPNDVFPEEFPRFLFVDLNQRRLFAKLHGNLYDAKYWQGLQEQIREGKVIDVFPYRRQETPEQLLK

aceK

Isocitrate dehydrogenase kinase/phosphatase

577 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

66.761 kDa

MVQSAPASEIAALILRGFDDYREQFREITDGARARFEQAQWQEAQRASTQRINLYEEKVAETVAGLRVGLADSELLDVERWPIIKSAYIAQIDLRLDDELAETWFNSIFCGLFSHDNISDGTMFVHTTRPSLRAHARAPYTRTYRPGGDLRQALEKIFDDYRFDVPYDDRERDLERIDALLHSNLPDWVCKDPDLAIELIGSVFYRNKGAYLVGRLFTPDEQWPLVFPLLHREGHGIQFDTVITDEAEVSIIFSFTRSYFMVDVPVPAELVAFLKRLLPGKHLAELYTSIGFYKQGKSEFYRALINHLATTDDRFVMAPGVRGMVMSVFTLPGFNTVFKIIKDRFNPSKSVDHATVIQKYQLVKNHDRVGRLADTQQFADFRFPVSKFEPECLAELLEVAPSTVVMEGDVVLIRHCWTERRMTPLNIYLENASEAQTREALNDYGLAIKQLAAANIFPGDMLLKNFGVTRHGRVVFYDYDEICYLTEVNFRYIPEPRFPEDEMSSEPWYSVGPNDVFPEEFPRFLFVDLNQRRLFAKLHGNLYDAKYWQGLQEQIREGKVIDVFPYRRQETPEQLLG

aceK

Isocitrate dehydrogenase kinase/phosphatase

577 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

66.761 kDa

MVQSAPASEIAALILRGFDDYREQFREITDGARARFEQAQWQEAQRASAQRINLYEEKVAETVAGLRAGLADSELLDVERWPIIKSAYIAQIDLRLDDELAETWFNSIFCGLFSHDNISDGTMFVHTTRPSLRAHARAPYTRTYRPGGDLRQALEKIFDDYRFDVPYDDRERDLERIDALLHSNLPDWVCKDPDLAIELIGSVFYRNKGAYLVGRLFTPDEQWPLVFPLLHREDHGIQFDTVITDEAEVSIIFSFTRSYFMVDVPVPAELVAFLKRLLPGKHLAELYTSIGFYKQGKSEFYRALINHLATTDDRFVMAPGVRGMVMSVFTLPGFNTVFKIIKDRFNPSKSVDHATVIQKYQLVKNHDRVGRLADTQQFADFRFPVSKFEPECLAELLEVAPSTVVMEGDVVLIRHCWTERRMTPLNIYLENASEAQTREALNDYGLAIKQLAAANIFPGDMLLKNFGVTRHGRVVFYDYDEICYLTEVNFRYIPEPRFPEDEMSSEPWYSVGPNDVFPEEFPRFLFVDLNQRRLFAKLHGNLYDAKYWQGLQEQIREGKVIDVFPYRRQETPEQLLG

aceK

Isocitrate dehydrogenase kinase/phosphatase

577 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.684 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKSRIHLYDHHVGLVVEQLRCITNGQSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFYPDHGWESLLMRVISDLPLRLRWQNKSRDIHYIIRHLTEMLGTDNLAESHLQVANELFYRNKAAWLVGKLNTPFGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPTLMELLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPSRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFSVRYRPQV

aceK

Isocitrate dehydrogenase kinase/phosphatase

575 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.234 kDa

MSRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKSRIHLYDHHVGLVVEQLRCITDGKSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFFPDHGWEPLLTRILSDLPLRLPWQNKSRDIHYIIAHLTETFGAEALHRSHLQVANELFYRNKAAWLVGKLLTPAGTLPFLLPIHRTDEGELFVDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLLYLANSDEQFIEAPGIRGMVMLVFTLPGFDRVFKIIKDRFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRRIAPALMTLLRQEAPEKIIDLGDQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPQARYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQTRIREGHVEDVYAYRRKQRFCFRFAA

aceK

Isocitrate dehydrogenase kinase/phosphatase

575 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.107 kDa

MTAAMEQLVAHTILQGFDAMYGRFLDVTAGAQERFEQQDWSSVHLALKKRISFYDHHVGLVTSQIQIMLGERYANRSFLMAVKSSYENLLLDYPRYEIAESFFNSVYCRIFEHRNINRDKLFVHSSQENRIPTYPTQLTRIYHAHSGLTSLFDRVLDDTPFTQVWEDKQRDTKLIINHLKQELGAAFNDETSLELIREPFYRNKAAYLIGKITLNHDGQYQTIPLVLPVLNNSNKQLYVDACICHVNDASIIFGFARSYFMVYAPAPGALVRFLSNLIPNKTNAELYTAIGCQKHGKTELYREFLTHLDNSDDQFVTAPGIKGMVMSVFTLPSYDFVFKIIKDKFAPQKDISHATVKEKYKLVKEHDRVGRMADTQEYRHFTFERHRFSDELLAELLAVAPSIIKVTSDQIIISHLYMERRMIPFNIYVEQANDDDLRDAVDEYGKAIKQLAAANIFPGDMLFKNFGVTRHKRVVFYDYDEISYMTEMNFRKIPEPRTPEDEMSAEPWYSVGIYDVFPEEFRTFLLINPKVKALFNELHSDLFEAKYWQSLQQNITHGQYEDVYPYRGVHRLRKT

aceK

Isocitrate dehydrogenase kinase/phosphatase

575 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.157 kDa

MQQPLEQAVAETILQRFESFYSRFLEITQGSKSRFENSDWLGVQLAGRERIRLYDHHVGATTALIKQMMGATLPSQALLKQVKGAFSDLLPKCENFEVAESFFNSVYRRIFRHRNIRDENLYIHPFRSRGEHPDLSALLRIYRTDLAHLPQTLSQLLGDYSFTLPYEDKQRDIVDIQRHLAENGPAILHDEPFAIELLKEVFYRNKGAYLVGLIRVKGQVFPFILPLLSTGQSIYVDTVIFEPELASIVFGFARAYFMVYAPMPALFVLFLRQIMPHKPDYEIYNAIGCQKHGKTELYRHYQQHLAQSREQFVIAPGIKGMVMSVFTLPSYDVVFKVIKDEFTPPKDVSHEQVKAKYRLVKQHDRVGRMADTQEFTNFEFPLDRISPELLAELKTVAPSALTLTDDKLVIKHLYTERKMIPLNLYLDKADEQQTRLALEEYGNAIKQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTECNFRQIPPPRYPEDEWSAEPWYSVAPNDIFPEEFATFLLQKPQVRDIMMQLHKELFDANYWKMLQSNIKEGVFEDVYPYRRKKRFKFQRGG

aceK

Isocitrate dehydrogenase kinase/phosphatase

575 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.385 kDa

MQQPLEQAVAETILQRFESFYSRFLEITQGSKSRFENSDWLGVQLAGRERIRLYDHHVGATTALIKQMMGEHHATQELLKRVKGAFSDLLPRCDNFEVAESFFNSVYRRIFRHRNIRDENLYIHPFRSRGEHPDLSALLRVYRTDLTHLPQTLSQMLGDYSFTLPYEDKQRDIVDIHRHLAENGPQILHEEPFAIELLKEVFYRNKGAYLVGLIRVKGQVFPFILPLLSTGQSIYVDTVIFEPELASIVVGFARAYFMVYAPVPALFVVFLRQIMPHKPDYEIYNAIGCQKHGKTELYRHYQQHLAQSREQFVIAPGIKGMVMSVFTLPSYDVVFKVIKDEFTPPKDVSHEQVRAKYRLVKQHDRVGRMADTQEFTNFEFPLDRISPELLAELKTVAPSALTITSDKLVIKHLYTERKMIPLNLYLDKADEQQTRLALEEYGNAIKQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTECNFRQIPPPRYPEDEWSAEPWYSVAPNDIFPEEFATFLLQKPQVREIMMQLHKEMFDANYWKMLQSNIKVGVFEDVYPYRRKKRFKFQRGG

aceK

Isocitrate dehydrogenase kinase/phosphatase

575 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

65.586 kDa

MAEPNDVAAAGAAAIAASFEAYQEERARITRRARERFEKRDWAAGQADARERLDLRDRLVNACVGTVRAELGGAAHDHGLWRAMKELYEARVESRPDREIGQSFFNSVTRRVFVTVGVDPAIEFLAADGPAVREGPVPVYARYRREVSTEALLRTVLRACAFAAPYEDLERDARIAAIELDSHLRELDDGQPIEALELVKAVFYRGKGAYLVGRLRRGRYTTPLVLALVHGERGVVLDAILFTQEDVSIVFSFTRSYFHVEVERPRELVAFLSTLLPLKRVSELYIALGFNKHGKTELYREIARHIAETGEAFVPARGDKGLVMSVFTLPGLDVVFKVIKDEFKPPKQTTRREVMDKYRHVFRHDRAGRLVDAQEFEHLAFPADRFSPEVLRELSEECRGSIEIGRAEISVKHLYAERRVTPLNLFIREADEWTARQAVLDFGRALKDLAATNTFPGDLLLKNFGVTRHGRVIFYDYDELTRVTDCVFRDLPTPSGDDEETSGEPWFYVGQDDVFPEELLPFLGLAGRLREVFLQAHGDLLTARYWRAIQERIREGEIVDIYPYREEQRLVHGYE

aceK

Isocitrate dehydrogenase kinase/phosphatase

575 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.387 kDa

MVTKLEQLIAQTILQGFDAQYGRFLEVTAGAQHRFEQADWHAVQQAMKKRIHLYDSHVGLVVEQLKHITDQRCFDVNFLTRVKEIYTGLLPDYPRFEIAESFFNSVYCRLFKHRDLTPDKLFVFSSQPERRFREIPRPLARDFAPKGDLSGMLQVVLNDLPLRLPWENLPRDIGYIATALRQNFTDEQLATARFQVANELFYRNKAAWLVGKLRLADEVYPFLLPIHHNESGGLFIDTCLTSKAEASIVFGFARSYFMVYAPLPAAMVEWLREILPGKSTAELYMAIGCQKHGKTESYREYLTFVHQSSEQFIIAPGVKGMVMLVFTLPSFDRVFKVIKDQFAPQKEVSQTRVLECYQLVKEHDRVGRMADTQEYENFVIDKHRISAELLTELQREVPEKLEDLGDQIIIKHLYMERRMTPLNLYIEQANDQQLKDAIEEYGNAIKQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDEMASEPWYSVSPNDVFPEEFRHFLCTDLKVRHFFEEMHSDLFHASYWRGLQQRIKDGHVEDVFAYRRKQRFSQRVIS

aceK

Isocitrate dehydrogenase kinase/phosphatase

575 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.622 kDa

MVAKLEQLIAQTILQGFDAQYGRFLEVTAGAQHRFEQADWHAVQQAMKKRIHLYDHHVGLVVEQLKYITDQRHFDVEFLARVKEIYTGLLPDYPRFEIAESFFNSVYCRLFKHRDLTPDKLFVFSSQPERRFREIPRPLARDFIPKGDLSGMLQMVLNDLSLRLHWENLSRDIDYIVMAIRQAFTDEQLASAHFQIANELFYRNKAAWLVGKLRLNGDIYPFLLPIHHNESGELFIDTCLTSKAEASIVFGFARSYFMVYVPLPAAMVEWLREILPGKSTAELYTAIGCQKHGKTESYREYLAFIHQSSEQFIIAPGVKGMVMLVFTLPSFDRVFKVIKDQFAPQKEVTQARVLECYQLVKEHDRVGRMADTQEYENFVIDKHRISPELLAELQHEVPEKLEDLGDKIVIKHLYMERRMTPLNLYMEQADDQQLKDAIEEYGNAIKQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDEMASEPWYSVSPNDVFPEEFRHFLCSDRKVRHFFEEMHGDLFQASYWRGLQQRIRDGHVEDVFAYRRKQRFSQRALN

aceK

Isocitrate dehydrogenase kinase/phosphatase

575 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.622 kDa

MVAKLEQLIAQTILQGFDAQYGRFLEVTAGAQHRFEQADWHAVQQAMKKRIHLYDHHVGLVVEQLKYITDQRHFDVEFLARVKEIYTGLLPDYPRFEIAESFFNSVYCRLFKHRDLTPDKLFVFSSQPERRFREIPRPLARDFIPKGDLSGMLQMVLNDLSLRLHWENLSRDIDYIVMAIRQAFTDEQLASAHFQIANELFYRNKAAWLVGKLRLNGDIYPFLLPIHHNESGELFIDTCLTSKAEASIVFGFARSYFMVYVPLPAAMVEWLREILPGKSTAELYTAIGCQKHGKTESYREYLAFIHQSSEQFIIAPGVKGMVMLVFTLPSFDRVFKVIKDQFAPQKEVTQARVLECYQLVKEHDRVGRMADTQEYENFVIDKHRISPELLAELQHEVPEKLEDLGDKIVIKHLYMERRMTPLNLYMEQADDQQLKDAIEEYGNAIKQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDEMASEPWYSVSPNDVFPEEFRHFLCSDRKVRHFFEEMHGDLFQASYWRGLQQRIRDGHVEDVFAYRRKQRFSQRALN

aceK

Isocitrate dehydrogenase kinase/phosphatase

575 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.622 kDa

MVAKLEQLIAQTILQGFDAQYGRFLEVTAGAQHRFEQADWHAVQQAMKKRIHLYDHHVGLVVEQLKYITDQRHFDVEFLARVKEIYTGLLPDYPRFEIAESFFNSVYCRLFKHRDLTPDKLFVFSSQPERRFREIPRPLARDFIPKGDLSGMLQMVLNDLSLRLHWENLSRDIDYIVMAIRQAFTDEQLASAHFQIANELFYRNKAAWLVGKLRLNGDIYPFLLPIHHNESGELFIDTCLTSKAEASIVFGFARSYFMVYVPLPAAMVEWLREILPGKSTAELYTAIGCQKHGKTESYREYLAFIHQSSEQFIIAPGVKGMVMLVFTLPSFDRVFKVIKDQFAPQKEVTQARVLECYQLVKEHDRVGRMADTQEYENFVIDKHRISPELLAELQHEVPEKLEDLGDKIVIKHLYMERRMTPLNLYMEQADDQQLKDAIEEYGNAIKQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDEMASEPWYSVSPNDVFPEEFRHFLCSDRKVRHFFEEMHGDLFQASYWRGLQQRIRDGHVEDVFAYRRKQRFSQRALN

aceK

Isocitrate dehydrogenase kinase/phosphatase

575 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.622 kDa

MVAKLEQLIAQTILQGFDAQYGRFLEVTAGAQHRFEQADWHAVQQAMKKRIHLYDHHVGLVVEQLKYITDQRHFDVEFLARVKEIYTGLLPDYPRFEIAESFFNSVYCRLFKHRDLTPDKLFVFSSQPERRFREIPRPLARDFIPKGDLSGMLQMVLNDLSLRLHWENLSRDIDYIVMAIRQAFTDEQLASAHFQIANELFYRNKAAWLVGKLRLNGDIYPFLLPIHHNESGELFIDTCLTSKAEASIVFGFARSYFMVYVPLPAAMVEWLREILPGKSTAELYTAIGCQKHGKTESYREYLAFIHQSSEQFIIAPGVKGMVMLVFTLPSFDRVFKVIKDQFAPQKEVTQARVLECYQLVKEHDRVGRMADTQEYENFVIDKHRISPELLAELQHEVPEKLEDLGDKIVIKHLYMERRMTPLNLYMEQADDQQLKDAIEEYGNAIKQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDEMASEPWYSVSPNDVFPEEFRHFLCSDRKVRHFFEEMHGDLFQASYWRGLQQRIRDGHVEDVFAYRRKQRFSQRALN

aceK

Isocitrate dehydrogenase kinase/phosphatase

575 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.622 kDa

MVAKLEQLIAQTILQGFDAQYGRFLEVTAGAQHRFEQADWHAVQQAMKKRIHLYDHHVGLVVEQLKYITDQRHFDVEFLARVKEIYTGLLPDYPRFEIAESFFNSVYCRLFKHRDLTPDKLFVFSSQPERRFREIPRPLARDFIPKGDLSGMLQMVLNDLSLRLHWENLSRDIDYIVMAIRQAFTDEQLASAHFQIANELFYRNKAAWLVGKLRLNGDIYPFLLPIHHNESGELFIDTCLTSKAEASIVFGFARSYFMVYVPLPAAMVEWLREILPGKSTAELYTAIGCQKHGKTESYREYLAFIHQSSEQFIIAPGVKGMVMLVFTLPSFDRVFKVIKDQFAPQKEVTQARVLECYQLVKEHDRVGRMADTQEYENFVIDKHRISPELLAELQHEVPEKLEDLGDKIVIKHLYMERRMTPLNLYMEQADDQQLKDAIEEYGNAIKQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDEMASEPWYSVSPNDVFPEEFRHFLCSDRKVRHFFEEMHGDLFQASYWRGLQQRIRDGHVEDVFAYRRKQRFSQRALN

aceK

Isocitrate dehydrogenase kinase/phosphatase

575 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.622 kDa

MVAKLEQLIAQTILQGFDAQYGRFLEVTAGAQHRFEQADWHAVQQAMKKRIHLYDHHVGLVVEQLKYITDQRHFDVEFLARVKEIYTGLLPDYPRFEIAESFFNSVYCRLFKHRDLTPDKLFVFSSQPERRFREIPRPLARDFIPKGDLSGMLQMVLNDLSLRLHWENLSRDIDYIVMAIRQAFTDEQLASAHFQIANELFYRNKAAWLVGKLRLNGDIYPFLLPIHHNESGELFIDTCLTSKAEASIVFGFARSYFMVYVPLPAAMVEWLREILPGKSTAELYTAIGCQKHGKTESYREYLAFIHQSSEQFIIAPGVKGMVMLVFTLPSFDRVFKVIKDQFAPQKEVTQARVLECYQLVKEHDRVGRMADTQEYENFVIDKHRISPELLAELQHEVPEKLEDLGDKIVIKHLYMERRMTPLNLYMEQADDQQLKDAIEEYGNAIKQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDEMASEPWYSVSPNDVFPEEFRHFLCSDRKVRHFFEEMHGDLFQASYWRGLQQRIRDGHVEDVFAYRRKQRFSQRALN

aceK

Isocitrate dehydrogenase kinase/phosphatase

574 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.148 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFHPDHGWESLLMRVISDLPLRLRWQNKSRDIHYIVRHLTETLGTDNLAESHLQVANELFYRNKAAWLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDRFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPALMALLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPLPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFSVRFV

aceK

Isocitrate dehydrogenase kinase/phosphatase

574 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.206 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFHPDHGWESLLMRVISDLPLRLRWQNKSRDIHYIVRHLTETLGTDNLAESHLQVANELFYRNKAAWLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDRFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPALMELLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPLPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFSVRFV

aceK

Isocitrate dehydrogenase kinase/phosphatase

574 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.206 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFHPDHGWESLLMRVISDLPLRLRWQNKSRDIHYIVRHLTETLGTDNLAESHLQVANELFYRNKAAWLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDRFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPALMELLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPLPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFSVRFV

aceK

Isocitrate dehydrogenase kinase/phosphatase

574 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.206 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFHPDHGWESLLMRVISDLPLRLRWQNKSRDIHYIVRHLTETLGTDNLAESHLQVANELFYRNKAAWLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDRFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPALMELLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPLPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFSVRFV

aceK

Isocitrate dehydrogenase kinase/phosphatase

574 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.206 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFHPDHGWESLLMRVISDLPLRLRWQNKSRDIHYIVRHLTETLGTDNLAESHLQVANELFYRNKAAWLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDRFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPALMELLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPLPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFSVRFV

aceK

Isocitrate dehydrogenase kinase/phosphatase

574 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.206 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFHPDHGWESLLMRVISDLPLRLRWQNKSRDIHYIVRHLTETLGTDNLAESHLQVANELFYRNKAAWLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDRFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPALMELLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPLPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFSVRFV

aceK

Isocitrate dehydrogenase kinase/phosphatase

574 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.127 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFHSDHGWESLLMRVISDLPLRLRWQNKSRDIHYIVRHLTETLGTDNLAESHLQVANELFYRNKAAWLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDRFAPQKEMSAAHVCACYQLVKEHDRVGRMADTQEFENFVLEKRHISPALMELLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFSVRFV

aceK

Isocitrate dehydrogenase kinase/phosphatase

574 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.206 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFHPDHGWESLLMRVISDLPLRLRWQNKSRDIHYIVRHLTETLGTDNLAESHLQVANELFYRNKAAWLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDRFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPALMELLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPLPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFSVRFV

aceK

Isocitrate dehydrogenase kinase/phosphatase

574 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

67.277 kDa

MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQLAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFHPDHGWESLLMRVISDLPLRLRWQNKSRDIHYIIRHLTETLGTDNLAESHLQVANELFYRNKAAWLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPALMELLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFSVRYGEMLF

aceK

Isocitrate dehydrogenase kinase/phosphatase

573 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

66.062 kDa

MPQQWPATDIARLILDGFDDYREHFRRITDGARERFEQARWQDTQTASAARINLYEEKVGETVARLREYFEPDTLMDVTCWPLVKSAYISIIDLRFDDELSETWYNSIFCSLFSHDLISDGCMFIHTTRPSLRRARAAQTRTYKPQGQISGMLASIFADYRFSEAYADLPGDLLRLEAQLRENLPDWVCKDPELSVELFSSVLYRNKGAYLVGRIYTNDDQWPLVIPLLHREGRGIQIDALITDEAEVSIIFSFTRSYFMVDVPVPAEFIGFLKRILPGKHIAELYTSIGFYKHGKSEFYRALINHLANTDDQFIMAPGVRGMVMSVFTLPGFNTVFKIIKDRFSPSKNVDRATVIEKYRLVKSVDRVGRMADTQEFADFRFPLSKFEPACLAELLEVAPSTVSLEGETVLIRHCWTERRMTPLNLYLDNANEAQVREALEDYGLAIKQLAAANIFPGDMLLKNFGVTRHGRVVFYDYDEICFLTEANFRHIPAPRTPEDEMASEPWYSIGPLDVFPEEFPPFLFADAAQRKLFDQLHGELYNADYWKGLQEAIRAGKVIDVFPYRRKGLDNE

aceK

Isocitrate dehydrogenase kinase/phosphatase

573 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

66.31 kDa

MVQHELAAEIARQILLGFDDYREHFRLITEGARARFEQAQWQEAQRASAARISLYEEKVGETRRRLLASFDHADLLQVEAWPQIKSAYIELINPRFDDELSETWYNSIFCGLFSHDCISDGTMFIHTTRPAVRAHERLAQTRRYRPNGDLRGMLEQILRDYAFSVPYCDLPGDLQRLQTQLCETLPDWVCKDPELTVEVFVSVLYRNKGAYLIGRIFTCDEQWPLAIPLLHRDGQGIVADALITDEAEVSIIFSFTRSYFMVEVPIPAEFVGFLKRILPGKHIAELYSSIGFYKHGKSEFYRALIDHLANTDDRFVMAPGVRGMVMTVFTLPGFNTVFKLIKDRFSPIKSVNRANVIEKYRLVKSVDRVGRMADTQEFADFRFPKAKFEPECLAELLEVAPSTVEVQGDTVLVRHCWTERRMTPLNLYLENASEQQVREALEDYGLAIKQLAAANIFPGDMLLKNFGVTRHGRVVFYDYDEISFLTEVNFRHIPPPRYPEDEMASEPWYSVGPNDVFPEEFPRFLFADLGQRRLFASLHGELYDADYWKGLQDAIRQGKVIDVFPYRRKADRN

aceK

Isocitrate dehydrogenase kinase/phosphatase

573 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

66.095 kDa

MSQSWPAADIARMILDGFDDYREHFRQITDGARQRFEQAQWQQAQKASAARINLYEEKVGETVARLHQAFSTESLMDVSQWPLVKSAYISLIDLRFDDELSETWYNSIFCGLFSHDLISDGCMFIHTTRPSLRRARAAQTRSYKPQGELATMLEQVFADYRFSEDYADLPGDLRRLEAQLRENLPDWVCKDPELTLELFSSVLYRNKGAYLVGRIFTHEEQWPLVIPLLHREGRGIQIDALITDEADVSIIFSFTRSYFMVDVPVPAEFIGFLKRILPGKHIAELYTSIGFYKHGKSEFYRALINHLASTDDRFIMAPGVRGMVMSVFTLPGFNTVFKIIKDRFSPSKNVDRATVIEKYRLVKSVDRVGRMADTQEFADFRFPLSKFDPACLEELLEVAPSTVAVEGQTVLIRHCWTERRMTPLNLYLEHANEAQVREALEDYGLAIKQLAAANIFPGDMLLKNFGVTRHGRVVFYDYDEICFLTEANFRHIPAPRTPEDEMASEPWYSIGPHDVFPEEFPPFLFADAGQRKLFDQLHGELYNADYWKGLQEAIRAGKVIDVFPYRRQGLEDE

aceK

Isocitrate dehydrogenase kinase/phosphatase

573 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

66.734 kDa

MSRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEHADWHAVQQAMKQRIHLYDHHVGLVVEQLRCITEGKSTDVDFLLRVKEHYTHLLPDYPRFEIAESFFNSVYCRLFDHRSLSPERLFIFSSQPARRFRAIPRPLAKDFFPEKGWEKALNNVLSDLPLRLPWQNKTRDVGYISAHLVETLGEETLRHSHLQVANELFFRNKAAWLVGKLITPDATLPFLLPIHRSDDGELFVDTCLTTSAEASIVFGFARSYFMVYAPFPAALVEWLREILPVKTTAELYMAIGCQKHAKTESYREYLYYITSTDEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDQFAPQKEMTAAHVRACYQLVKEHDRVGRMADTQEFENFVLDKRQIDPTLMALLLQEAPDKITDLGDKIAISHLYIERRMVPLNIWLEQVEGAQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRTIPAARYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHDDLFRADYWRSLQTRIKEGHVEDVYAYRKRQRFCLRG

aceK

Isocitrate dehydrogenase kinase/phosphatase

572 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

66.068 kDa

MGQQWPAGEIARLILDGFDDYREHFRQITDGARVRFEQAQWQEAQRASAARINLYEEKVAQTRERLLEGFDESLLEVGQWPLVKSAYIALIDLRFDDELAETWFNSIFCSLFSHDLISDGCMFIHTTRPSLRNQPSAAQTRNYRPAGELHLALQAIFDDYRFDVSYEDLPRDLQRLEGQLRASLPDWICKDPQQCIELFSSVLYRNKGAYLVGRIYTPDEQWPLVIPLLHREGLGIQVDAAITDEAEVSIIFSFTRSYFMVDVAIPAEFVGFLKRILPGKHIAELYTSIGFYKHGKSEFYRALIGHLASTDDRFIMAPGVRGMVMSVFTLPGFNTVFKIIKDRFAHAKTVDRKTVIEKYRLVKSVDRVGRMADTQEFSDFRFPKAKFEPECLAELLEVAPSTVVVEGDTVLVRHCWTERRMTPLNLYLESASEAQVREALDDYGLAIKQLAAANIFPGDMLLKNFGVTRHGRVVFYDYDEICFLTEVNFRRIPPPRFPEDEMSSEPWYSVGPMDVFPEEFPPFLFADIKQRRLFSQLHGNLYDADYWKQLQDAIRAGKVIDVFPYRRKSPVE

aceK

Isocitrate dehydrogenase kinase/phosphatase

571 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

65.954 kDa

MSQPWPAVEIARMILAGFDDYRDHFQRITLGARQRFEQARWQDIQQAAAARINLYEEKVAEVNGWLRQAFAAEVLLDVEQWPLVKNAYIHLIDPRLDDELAETWYNSLFCSLFSHDLISDGCMFIHTTRPSMRGRERAAQTRTYRLDGSLRNLLRAVFADYPFDMPYGDLEGDLARLEEQLRECLPDWVCKDPALAVELFVPVLYRNKGAYLVGRLYNSDEQWPLVIPLLHREGHGIEADALITDEAEVSIIFSFTRSYFMADVPVPAEFVNFLKRILPGKHIAELYTSIGFYKQGKSEFYRALINHLASSDDRFVMAPGVRGMVMSVFTLPGFNTVFKIIKDRFSPSKTVDRATVIDKYRLVKSVDRVGRMADTQEFADFRFPRSKFEPDCLAELLEVAPSTVALEGDTVLIRHCWTERRMTPLNLYLEQATEGQVLEALEDYGLAIKQLAAANIFPGDMLLKNFGVTRHGRVVFYDYDEISFLTEVNFRHIPPPRYPEDEMSGEPWYSIGPHDVFPEEFPPFLFADMGQRRLFSRLHGELYDADYWKGLQAAIREGKVIDVFPYRRKAR

aceK

Isocitrate dehydrogenase kinase/phosphatase

571 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

66.183 kDa

MSQPWPAAEIARVILDGFDDYREHFRRITLGARERFEQARWQDIQRAAAARINLYEEKVAEVNGWLRKGFEGQVLLDVEQWPLVKNAYIRLIDPRLDDELSETWYNSLFCSLFSHDQISDGCMFIHTTRPSMRVHERAAQTRTYALTDRLKGLLRAIFADYAFDVPYGDLEADLSRLEEQLRECLPDWVCKDPQLKIELFTPVLYRNKGAYLVGRLYTPDEQWPLVIPLLHREGHGIEADALITDEAEVSIIFSFTRSYFMVDVPVPGEFVNFLKRILPGKHIAELYTSIGFYKHGKSEFYRALINHLANSDDRFVMAPGVRGMVMSVFTLPGFNTVFKIIKDRFSPSKTVDRATVIEKYRLVKSVDRVGRMADTQEFADFRFPQGKFDPECLAELLEVAPSTVSLEGDTVLIRHCWTERRMTPLNLYLEHASEGQVLEALEDYGLAIKQLAAANIFPGDMLLKNFGVTRHGRVVFYDYDEISFLTEVNFRHIPPPRYPEDEMSGEPWYSIGPHDVFPEEFPPFLFADIGQRRLFSRLHGELYDADYWKGLQEAIRAGKVIDVFPYRRKSR

aceK

Isocitrate dehydrogenase kinase/phosphatase

571 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

65.954 kDa

MSQPWPAVEIARMILAGFDDYRDHFQRITLGARQRFEQARWQDIQQAAAARINLYEEKVAEVNGWLRQAFAAEVLLDVEQWPLVKNAYIHLIDPRLDDELAETWYNSLFCSLFSHDLISDGCMFIHTTRPSMRGRERAAQTRTYRLDGSLRNLLRAVFADYPFDMPYGDLEGDLARLEEQLRECLPDWVCKDPALAVELFVPVLYRNKGAYLVGRLYNSDEQWPLVIPLLHREGHGIEADALITDEAEVSIIFSFTRSYFMADVPVPAEFVNFLKRILPGKHIAELYTSIGFYKQGKSEFYRALINHLASSDDRFVMAPGVRGMVMSVFTLPGFNTVFKIIKDRFSPSKTVDRATVIDKYRLVKSVDRVGRMADTQEFADFRFPRSKFEPDCLAELLEVAPSTVALEGDTVLIRHCWTERRMTPLNLYLEQATEGQVLEALEDYGLAIKQLAAANIFPGDMLLKNFGVTRHGRVVFYDYDEISFLTEVNFRHIPPPRYPEDEMSGEPWYSIGPHDVFPEEFPPFLFADMGQRRLFSRLHGELYDADYWKGLQAAIREGKVIDVFPYRRKAR

aceK

Isocitrate dehydrogenase kinase/phosphatase

569 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

65.953 kDa

MTQHWPAGEIARMILDGFDDYREHFRRITLGARERFEQARWQDIQRAAAARINLYEQKVGEVNGWLRDAFDDEVLLEVEQWPLVKSAYIRLIDPRLDDELSETWYNSLFCSLFSHDQISDGCMFIHTTRPSIRSHQRAAQTRTYCLDASLQSLLRAIFADYAFAYGDLESDVSRLEAQLREHLPDWVCKDSTLTVELFSPVLYRNKGAYLVGRLYNSDEQWPLVIPLLHREGHGVEADALITDEAEVSIIFSFTRSYFMVDVPVPAEFVNFLKRILPGKHIAELYTSIGFYKHGKSEFYRALINHLANSDDRFIMAPGVRGMVMSVFTLPGFNTVFKIIKDRFSPSKTVDRATVIDKYRLVKSVDRVGRMADTQEFADFRFPRDKFEPECLAELLEVAPSTVVLEGDTVLIRHCWTERRMTPLNLYLEHASEGQVLEALEDYGLAIKQLAAANIFPGDMLLKNFGVTRHGRVVFYDYDEISFLTEVNFRHIPPPRYPEDEMSGEPWYSIGPHDVFPEEFPPFLFADMGQRRLFSRLHGELYDADYWKGLQAAIREGKVIDVFPYRRKGR

aceK

Isocitrate dehydrogenase kinase/phosphatase

569 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

65.929 kDa

MTQHWPAGEIARMILDGFDDYREHFRRITLGARERFEQARWQDIQRAAAARINLYEQKVGEVNGWLRDGFDEEVLLEVEQWPLVKSAYIRLIDPRLDDELAETWYNSLFCSLFSHDQISDGCMFIHTTRPSIRSHERAAQTRTYMPDGSLKGLVRAIFRDYAFDYGDLESDLSRLEEQLRDCLPDWVCKDPALAVELFVPVLYRNKGAYLVGRLYNSDEQWPLVIPLLHREGHGIEADALITDEAEVSIIFSFTRSYFMVDVPVPAEFVNFLKRILPGKHIAELYTSIGFYKHGKSEFYRALINHLASTDDRFIMAPGVRGMVMSVFTLPGFNTVFKIIKDRFSPSKTVDRATVIDKYRLVKSVDRVGRMADTQEFADFRFPRGKFEPECLAELLEVAPSTVAVEGDTVLVRHCWTERRMIPLNLYLEQASEGQVLEALEDYGLAIKQLAAANIFPGDMLLKNFGVTRHGRVVFYDYDEISYLTEVNFRHIPPPRYPEDEMSGEPWYSIGPHDVFPEEFPPFLFADMGQRRLFSRLHGELYDADYWKGLQASIREGKVIDVFPYRRKGR

aceK

Isocitrate dehydrogenase kinase/phosphatase

564 amino acids

Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.

Belongs to the AceK family.

65.928 kDa

MTISPETLAKSILDGFHSHYRRFQVLTQGARERFLKRDWTAVVSAASERIHYYDHQVGTTAKKVERRVGTELDEGLWLATRQRYQQLLKFHPQAELAETFYNSVFCRVFDRAYFNNDYIFVETVLANHIPVPVENECHSYFPVVDGLEGTLTRVFEDIGLGGEFENFENDIEQLRDKFFERATETDIEAHNLRIDVLKSPFYRNKAAYIVGRVVTENNHYPFIVPVLINSQGKLYVDAFITRSDRMATIFGFARSYFMVETEAPSALVRFLKDLMPHKTLAELYSSVGFHKQGKTEFYREFLHHLRRTDDQLSAAPGVKGMVMTVFTLPSFPYVFKVIKDRLGGTKEFGRQTVIDRYRMVKRHDRVGRMADTLEFVDVALPLKRISADLLDEFKQTIANSISIEGDTLVIHQLFVERRMTPLNLYLEYANDEEVDAAMDDYGRALKEMMAANIFPGDMLLKNFGVTRHKRVVFYDYDEVRYLTDMSFRRLPENDWEVSYAPDDVFPQQLAQFAVPQAKYRNKLLKRHPELIDSAYWCRVQKNIRKGELTDVFPYDADLRFTRRF