dld

Delta-like protein D

717 amino acids

Acts as a ligand for Notch receptors and is involved in primary neurogenesis and somitogenesis. Can activate Notch receptors, thereby playing a key role in lateral inhibition, a process that prevents the immediate neighbors of each nascent neural cell from simultaneously embarking on neural differentiation. Required in somite segmentation to keep the oscillations of neighboring presomitic mesoderm cells synchronized.

79.061 kDa

MGRLMIAVLLCVMISQGFCSGVFELKLQEFLNKKGVTGNANCCKGSAAEGHQCECKTFFRICLKHYQANVSPDPPCTYGGAVTPVLGSNSFQVPESFPDSSFTNPIPFAFGFTWPGTFSLIIEALHTDSTDDLSTENPDRLISRMTTQRHLTVGEEWSQDLQVGGRTELKYSYRFVCDEHYYGEGCSVFCRPRDDTFGHFTCGERGEIICNSGWKGQYCTEPICLPGCDEDHGFCDKPGECKCRVGFSGKYCDDCIRYPGCLHGTCQQPWQCNCQEGWGGLFCNQDLNYCTHHKPCQNGATCTNTGQGSYTCSCRPGFTGDSCEIEVNECSGSPCRNGGSCTDLENTYSCTCPPGFYGRNCELSAMTCADGPCFNGGHCADNPEGGYFCQCPMGYAGFNCEKKIDHCSSNPCSNDAQCLDLVDSYLCQCPEGFTGTHCEDNIDECATYPCQNGGTCQDGLSDYTCTCPPGYTGKNCTSAVNKCLHNPCHNGATCHEMDNRYVCACIPGYGGRNCQFLLPENPQGQAIVEGADKRYSYEEDDGGFPWTAVCAGIILVLLVLIGGSVFVIYIRLKLQQRSQQIDSHSEIETMNNLTNNRSREKDLSVSIIGATQVKNINKKVDFQSDGDKNGFKSRYSLVDYNLVHELKQEDLGKEDSERSEATKCEPLDSDSEEKHRNHLKSDSSERKRTESLCKDTKYQSVFVLSEEKDECIIATEV

dld

Quinone-dependent D-lactate dehydrogenase

571 amino acids

Catalyzes the oxidation of D-lactate to pyruvate. Has also weak activity with L-lactate and DL-2-hydroxybutyrate. Electrons derived from D-lactate oxidation enter the electron transport chain. Essential for growth with D-lactate as sole carbon and energy source.

Belongs to the quinone-dependent D-lactate dehydrogenase family.

63.723 kDa

MTQPGQTTTTSHEAIDAFKRIVGDEHVLTSERATMPFSKGYRFGGGPVFAVVRPGTLVEMWRALQVSVDNNLIVIPQASNTGLTGGSGPGFQDYDRPIVIISTHRIDEVHLINDAREAISLAGTPLTHLTDALAKHQREPHSVIGSTSIGASVIGGIANNSGGSQIRKGPAFTREAIFARVNDDGKVELVNHLGISLGDDPEVALDRLQRGEWSPEDVTPAPEDSNETEYAEHLRKIVPSPARYNANPEYLFEASGSAGKLMVFAVRTRTFPREVHPTVFYIGTNNTHELEEIRRLFLEADMPLPISGEYMGRSAFDLAEKYGKDTFVFLKFMSPALQTRMFSFKTWANGLFSKIPGIGPTFADTVSQAMFSVLPNQLPKRMMEYRNRFEHHLLLTVSESQKAASEKMLKEFFAEPEHTGEFFICTSDEEKSASLNRFGAASAATRYAALKRRHIAGLIPIDVALRRDDWNWLEVLPEEIDDQLEVKAYYGHFFCHVMHQDYVAKQGVDLEALHDRIQHLLEERGAKLPAEHNYGRIYKLPESMEEHFKELDPTNTFNAGIGGTSPHKDWA

dld

Quinone-dependent D-lactate dehydrogenase

571 amino acids

Catalyzes the oxidation of D-lactate to pyruvate. Electrons derived from D-lactate oxidation are transferred to the ubiquinone/cytochrome electron transfer chain, where they may be used to provide energy for the active transport of a variety of amino acids and sugars across the membrane.

Belongs to the quinone-dependent D-lactate dehydrogenase family.

64.612 kDa

MSSMTTTDNKAFLNELARLVGSSHLLTDPAKTARYRKGFRSGQGDALAVVFPGSLLELWRVLKACVTADKIILMQAANTGLTEGSTPNGNDYDRDVVIISTLRLDKLHVLGKGEQVLAYPGTTLYSLEKALKPLGREPHSVIGSSCIGASVIGGICNNSGGSLVQRGPAYTEMSLFARINEDGKLTLVNHLGIDLGETPEQILSKLDDDRIKDDDVRHDGRHAHDYDYVHRVRDIEADTPARYNADPDRLFESSGCAGKLAVFAVRLDTFEAEKNQQVFYIGTNQPEVLTEIRRHILANFENLPVAGEYMHRDIYDIAEKYGKDTFLMIDKLGTDKMPFFFNLKGRTDAMLEKVKFFRPHFTDRAMQKFGHLFPSHLPPRMKNWRDKYEHHLLLKMAGDGVGEAKSWLVDYFKQAEGDFFVCTPEEGSKAFLHRFAAAGAAIRYQAVHSDEVEDILALDIALRRNDTEWYEHLPPEIDSQLVHKLYYGHFMCYVFHQDYIVKKGVDVHALKEQMLELLQQRGAQYPAEHNVGHLYKAPETLQKFYRENDPTNSMNPGIGKTSKRKNWQEVE

dld

Quinone-dependent D-lactate dehydrogenase

571 amino acids

Catalyzes the oxidation of D-lactate to pyruvate. Has also weak activity with L-lactate and DL-2-hydroxybutyrate. Electrons derived from D-lactate oxidation enter the electron transport chain. Essential for growth with D-lactate as sole carbon and energy source.

Belongs to the quinone-dependent D-lactate dehydrogenase family.

63.723 kDa

MTQPGQTTTTSHEAIDAFKRIVGDEHVLTSERATMPFSKGYRFGGGPVFAVVRPGTLVEMWRALQVSVDNNLIVIPQASNTGLTGGSGPGFQDYDRPIVIISTHRIDEVHLINDAREAISLAGTPLTHLTDALAKHQREPHSVIGSTSIGASVIGGIANNSGGSQIRKGPAFTREAIFARVNDDGKVELVNHLGISLGDDPEVALDRLQRGEWSPEDVTPAPEDSNETEYAEHLRKIVPSPARYNANPEYLFEASGSAGKLMVFAVRTRTFPREVHPTVFYIGTNNTHELEEIRRLFLEADMPLPISGEYMGRSAFDLAEKYGKDTFVFLKFMSPALQTRMFSFKTWANGLFSKIPGIGPTFADTVSQAMFSVLPNQLPKRMMEYRNRFEHHLLLTVSESQKAASEKMLKEFFAEPEHTGEFFICTSDEEKSASLNRFGAASAATRYAALKRRHIAGLIPIDVALRRDDWNWLEVLPEEIDDQLEVKAYYGHFFCHVMHQDYVAKQGVDLEALHDRIQHLLEERGAKLPAEHNYGRIYKLPESMEEHFKELDPTNTFNAGIGGTSPHKDWA

dld

Quinone-dependent D-lactate dehydrogenase

571 amino acids

Catalyzes the oxidation of D-lactate to pyruvate. Electrons derived from D-lactate oxidation are transferred to the ubiquinone/cytochrome electron transfer chain, where they may be used to provide energy for the active transport of a variety of amino acids and sugars across the membrane.

Belongs to the quinone-dependent D-lactate dehydrogenase family.

64.612 kDa

MSSMTTTDNKAFLNELARLVGSSHLLTDPAKTARYRKGFRSGQGDALAVVFPGSLLELWRVLKACVTADKIILMQAANTGLTEGSTPNGNDYDRDVVIISTLRLDKLHVLGKGEQVLAYPGTTLYSLEKALKPLGREPHSVIGSSCIGASVIGGICNNSGGSLVQRGPAYTEMSLFARINEDGKLTLVNHLGIDLGETPEQILSKLDDDRIKDDDVRHDGRHAHDYDYVHRVRDIEADTPARYNADPDRLFESSGCAGKLAVFAVRLDTFEAEKNQQVFYIGTNQPEVLTEIRRHILANFENLPVAGEYMHRDIYDIAEKYGKDTFLMIDKLGTDKMPFFFNLKGRTDAMLEKVKFFRPHFTDRAMQKFGHLFPSHLPPRMKNWRDKYEHHLLLKMAGDGVGEAKSWLVDYFKQAEGDFFVCTPEEGSKAFLHRFAAAGAAIRYQAVHSDEVEDILALDIALRRNDTEWYEHLPPEIDSQLVHKLYYGHFMCYVFHQDYIVKKGVDVHALKEQMLELLQQRGAQYPAEHNVGHLYKAPETLQKFYRENDPTNSMNPGIGKTSKRKNWQEVE

DLD

D-lactate dehydrogenase [cytochrome], mitochondrial

567 amino acids

Catalyzes the stereospecific oxidation of D-lactate to pyruvate. Involved in the detoxification of methylglyoxal and D-lactate, but probably not involved in the metabolization of glycolate.

Belongs to the FAD-binding oxidoreductase/transferase type 4 family.

62.176 kDa

MAFASKFARSKTILSFLRPCRQLHSTPKSTGDVTVLSPVKGRRRLPTCWSSSLFPLAIAASATSFAYLNLSNPSISESSSALDSRDITVGGKDSTEAVVKGEYKQVPKELISQLKTILEDNLTTDYDERYFHGKPQNSFHKAVNIPDVVVFPRSEEEVSKILKSCNEYKVPIVPYGGATSIEGHTLAPKGGVCIDMSLMKRVKALHVEDMDVIVEPGIGWLELNEYLEEYGLFFPLDPGPGASIGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAAGYDLTRLIIGSEGTLGVITEITLRLQKIPQHSVVAVCNFPTVKDAADVAIATMMSGIQVSRVELLDEVQIRAINMANGKNLTEAPTLMFEFIGTEAYTREQTQIVQQIASKHNGSDFMFAEEPEAKKELWKIRKEALWACYAMAPGHEAMITDVCVPLSHLAELISRSKKELDASSLLCTVIAHAGDGNFHTCIMFDPSSEEQRREAERLNHFMVHSALSMDGTCTGEHGVGTGKMKYLEKELGIEALQTMKRIKKTLDPNDIMNPGKLIPPHVCF

DLD

D-lactate dehydrogenase [cytochrome], mitochondrial

567 amino acids

Catalyzes the stereospecific oxidation of D-lactate to pyruvate. Involved in the detoxification of methylglyoxal and D-lactate, but probably not involved in the metabolization of glycolate.

Belongs to the FAD-binding oxidoreductase/transferase type 4 family.

62.176 kDa

MAFASKFARSKTILSFLRPCRQLHSTPKSTGDVTVLSPVKGRRRLPTCWSSSLFPLAIAASATSFAYLNLSNPSISESSSALDSRDITVGGKDSTEAVVKGEYKQVPKELISQLKTILEDNLTTDYDERYFHGKPQNSFHKAVNIPDVVVFPRSEEEVSKILKSCNEYKVPIVPYGGATSIEGHTLAPKGGVCIDMSLMKRVKALHVEDMDVIVEPGIGWLELNEYLEEYGLFFPLDPGPGASIGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAAGYDLTRLIIGSEGTLGVITEITLRLQKIPQHSVVAVCNFPTVKDAADVAIATMMSGIQVSRVELLDEVQIRAINMANGKNLTEAPTLMFEFIGTEAYTREQTQIVQQIASKHNGSDFMFAEEPEAKKELWKIRKEALWACYAMAPGHEAMITDVCVPLSHLAELISRSKKELDASSLLCTVIAHAGDGNFHTCIMFDPSSEEQRREAERLNHFMVHSALSMDGTCTGEHGVGTGKMKYLEKELGIEALQTMKRIKKTLDPNDIMNPGKLIPPHVCF

dld

Quinone-dependent D-lactate dehydrogenase

564 amino acids

Catalyzes the oxidation of D-lactate to pyruvate.

Belongs to the quinone-dependent D-lactate dehydrogenase family.

64.126 kDa

MSVQQLISRLTDIVGSRYIITDPTKTEAYRSGYRFGTGNALAVVRPATLLEFWNIVKVCVEHDVIVINQAANTGLTGGSTPDGNDYDRDIVVINTMRIDGIQLINNASQVICLPGSTLNELENQLKPFGREPHSVIGSSCIGASVIGGICNNSGGALVQRGPAYTEMALYAQLNEKGELELKNHLGIDLGETPEEILTNLQEKRYQVKDIRQDCGHGHDHYYCNYVRQVDEGSPARFNADPARHYEASGCAGKLAVFAVRLDTFPLEKETAVFYIGTNQTSVLSDIRRHMLVNFEVLPISGEYIHRDAFDIAAKYGKDTFWVIKKFGTHWLPKLFSLKSNVDRIGKKFFFLPQHLSDKFMQTVSKFIPEHLPQSLWDYRNKYEHHLIIKMGGKGIQEAREYLESYIADGSKGGYFECNAIETQAAMLHRFAVASAAIRYRAIHEKEVEEIVALDVALRRNDQDWFEVLPPEIDNRIISKLYYGHFMCHVFHQDYIVKKGYDYEELEYEMLKLLDKRGAQYPAEHNVGHLYEAKPTLRKFYKELDPTNSFNPGIGKTTRKKYWAE

dld

Quinone-dependent D-lactate dehydrogenase

564 amino acids

Catalyzes the oxidation of D-lactate to pyruvate.

Belongs to the quinone-dependent D-lactate dehydrogenase family.

64.126 kDa

MSVQQLISRLTDIVGSRYIITDPTKTEAYRSGYRFGTGNALAVVRPATLLEFWNIVKVCVEHDVIVINQAANTGLTGGSTPDGNDYDRDIVVINTMRIDGIQLINNASQVICLPGSTLNELENQLKPFGREPHSVIGSSCIGASVIGGICNNSGGALVQRGPAYTEMALYAQLNEKGELELKNHLGIDLGETPEEILTNLQEKRYQVKDIRQDCGHGHDHYYCNYVRQVDEGSPARFNADPARHYEASGCAGKLAVFAVRLDTFPLEKETAVFYIGTNQTSVLSDIRRHMLVNFEVLPISGEYIHRDAFDIAAKYGKDTFWVIKKFGTHWLPKLFSLKSNVDRIGKKFFFLPQHLSDKFMQTVSKFIPEHLPQSLWDYRNKYEHHLIIKMGGKGIQEAREYLESYIADGSKGGYFECNAIETQAAMLHRFAVASAAIRYRAIHEKEVEEIVALDVALRRNDQDWFEVLPPEIDNRIISKLYYGHFMCHVFHQDYIVKKGYDYEELEYEMLKLLDKRGAQYPAEHNVGHLYEAKPTLRKFYKELDPTNSFNPGIGKTTRKKYWAE

DLD

Dihydrolipoyl dehydrogenase, mitochondrial

509 amino acids

Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex) (By similarity). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion (By similarity). A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (By similarity). In monomeric form may have additional moonlighting function as serine protease (PubMed:17404228). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity).

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

54.185 kDa

MQSWSRVYCTLAKRGHFNRIAHGLQGVSAVPLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEMSEVRLNLEKMMEQKSNAVKALTGGIAHLFKQNKVVRVNGYGKITGKNQVTATKADGSTEVINTKNILIATGSEVTPFPGITIDEDTVVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVELLGHVGGIGIDMEVSKNFQRILQKQGFKFKLNTKVIGATKKSDGNIDVSIEAASGGKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHIIGPGAGEMINEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASFGKAINF

DLD

Dihydrolipoyl dehydrogenase, mitochondrial

509 amino acids

Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A. In monomeric form may have additional moonlighting function as serine protease (By similarity). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity).

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

54.121 kDa

MQSWSRVYCSLAKRGHFNRISHGLQGLSAVPLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCVEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEMSEVRLNLDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKNILIATGSEVTPFPGIMIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSIEAASGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGGMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASFGKSINF

Dld

Dihydrolipoyl dehydrogenase, mitochondrial

509 amino acids

Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A. In monomeric form may have additional moonlighting function as serine protease (By similarity). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity).

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

54.038 kDa

MQSWSRVYCSLAKKGHFNRLSHGLQGASSVPLRTYSDQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHLAHGKDFASRGIEIPEVRLNLEKMMEQKRSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTATTADGSTQVIGTKNILIATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGIGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSVEAASGGKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNTRFQTKIPNIFAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGVEFKVGKFPFAANSRAKTNADTDGMVKILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVARVCHAHPTLSEAFREANLAASFGKPINF

DLD

Dihydrolipoyl dehydrogenase, mitochondrial

509 amino acids

Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A. In monomeric form may have additional moonlighting function as serine protease (By similarity). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity).

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

54.153 kDa

MQSWSRVYCSLAKRGHFSRISHGLQAVSAVPLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCVEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEMSEVRLNLEKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTAKKADGSTQVIDTKNILIATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSIEGASGGKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVPIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASFGKSINF

DLD

Dihydrolipoyl dehydrogenase, mitochondrial

509 amino acids

Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A. In monomeric form may have additional moonlighting function as serine protease (By similarity). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity).

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

54.131 kDa

MQSWSRVYCSLAKRGHFNRISHGLQGVSSVPLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNDTLGGTCLNVGCIPSKALLNNSHYYHLAHGRDFASRGIELSEVRLNLEKMMEQKSSAVKALIGGIAHLFKQNKVVHVNGFGKITGKNQVTATKADGSSQVIGTKNILIATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGIGIDMEISKNFQRILQKQGFKFKLNTKVTGATKRSDGKIDVSVEAASGGKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASFGKPINF

DLD

Dihydrolipoyl dehydrogenase, mitochondrial

509 amino acids

Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex) (PubMed:15712224, PubMed:16442803, PubMed:16770810, PubMed:17404228, PubMed:20160912, PubMed:20385101). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion (PubMed:29211711). A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (PubMed:29211711). In monomeric form may have additional moonlighting function as serine protease (PubMed:17404228). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity).

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

54.177 kDa

MQSWSRVYCSLAKRGHFNRISHGLQGLSAVPLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEMSEVRLNLDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKNILIATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSIEAASGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASFGKSINF

DLD

Dihydrolipoyl dehydrogenase, mitochondrial

509 amino acids

Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A. In monomeric form may have additional moonlighting function as serine protease (By similarity). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity).

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

54.221 kDa

MQSWSRVYCSLAKRGHFNRISHGLQGLSAVPLRTYADQLIDADVTVIGSGPGGYVAAIKAAQLGFKTVCVEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEMSEVRLNLDKMMEQKSTAVKALTGGIAHLFKQNKVIHVNGYGKITGKNQVTATKVDGGTQVVDTKNILIATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGIGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSIEAASGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASFGKSINF

Dld

Dihydrolipoyl dehydrogenase, mitochondrial

509 amino acids

Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex) (By similarity). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion (By similarity). A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (By similarity). In monomeric form may have additional moonlighting function as serine protease (PubMed:17404228). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity).

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

54.272 kDa

MQSWSRVYRSLAKKGHFNRISHGLQGVSSVPLRTYADQPIEADVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEIPEVRLNLEKMMEQKHSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTATKADGSTQVIDTKNILVATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGIGIDMEISKNFQRILQRQGFKFKLNTKVTGATKKSDGKIDVSVEAASGGKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNNRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEFKIGKFPFAANSRAKTNADTDGMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAAAFGKPINF

DLD

Dihydrolipoyl dehydrogenase, mitochondrial

479 amino acids

Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex) (PubMed:15888450). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion (By similarity). A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (By similarity). In monomeric form may have additional moonlighting function as serine protease (By similarity). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (PubMed:14645106, PubMed:15888450).

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

50.723 kDa

single

FNRXSPGLQGVSSVPLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHLAHGKDFASRGIELSEVRLNLEKMMEQKSSAVKALTGGIAHLFKQNKVVHVNGFGNITGKNQVTATKADGSSQVIGTKNILIATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGAEVTAVEFLGHVGGIGIDMEISKKFQRILQKQGFKFKLNPKVPGATKRSDGKIDVSVEAAPGGKAEVIPCDVLLVCIGRRPFTQNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFR

dld

D-lactate dehydrogenase (acceptor)

443 amino acids

Converts D-lactate to pyruvate. Cannot use NAD(+), cytochrome C, methylene blue or dimethylnaphthoquinone as acceptors. Active in vitro with artificial electron acceptors such as 2,6-dichlorophenolindophenol, but the physiological acceptor is not yet known.

48.487 kDa

MSWIDELSKIVEVFPPSDAYRFDETPPLVAPRAAENFVVVKPSNSEEVSAILKFANEKSIPVFMRGGGTGLSGGAVPTEEGIVLSTEKMTELEVDADNRVAICGAGVTLKQLDDAAFRHGLSFPPHPGAETATVGGMIATNAGGVRALKYGTMRNYVLSLEAVLADGRIINVGGKTIKNSSGYSLLHLLVGSEGTLAVITKATIRLFPQMRDMTVLAIPFPTMEDAMNCVVEVARKMLPMALEFMEKRAVEIGEKVSGERWVSREGEAHLLMVFESFDEAEEAAKIAQSLGAIDVYAATTKKDQDRLLKVRGMIYEGLRKEVIEVLDACVPPAKIAEYWRRSNELAEEYGIELITYGHAGDGNVHQHPLVYEGWEKSYFEFRKSLLSLAVSLGGVISGEHGIGAVKLSELEELFPEQFELMRQIKLLFDPKNILNPGKVVRKL

dld

D-lactate dehydrogenase (acceptor)

443 amino acids

Converts D-lactate to pyruvate. Cannot use NAD(+), cytochrome C, methylene blue or dimethylnaphthoquinone as acceptors. Active in vitro with artificial electron acceptors such as 2,6-dichlorophenolindophenol, but the physiological acceptor is not yet known.

48.487 kDa

MSWIDELSKIVEVFPPSDAYRFDETPPLVAPRAAENFVVVKPSNSEEVSAILKFANEKSIPVFMRGGGTGLSGGAVPTEEGIVLSTEKMTELEVDADNRVAICGAGVTLKQLDDAAFRHGLSFPPHPGAETATVGGMIATNAGGVRALKYGTMRNYVLSLEAVLADGRIINVGGKTIKNSSGYSLLHLLVGSEGTLAVITKATIRLFPQMRDMTVLAIPFPTMEDAMNCVVEVARKMLPMALEFMEKRAVEIGEKVSGERWVSREGEAHLLMVFESFDEAEEAAKIAQSLGAIDVYAATTKKDQDRLLKVRGMIYEGLRKEVIEVLDACVPPAKIAEYWRRSNELAEEYGIELITYGHAGDGNVHQHPLVYEGWEKSYFEFRKSLLSLAVSLGGVISGEHGIGAVKLSELEELFPEQFELMRQIKLLFDPKNILNPGKVVRKL