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aas

Gene
aas
Protein
Bifunctional protein Aas
Organism
Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672)
Length
738 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
81.428 kDa
Sequence
MIHTLLRWVFQRLYRIRIEGDSSQFQQSKLLITPNHVSFLDGVLLALFLPIKPVFAVYSSISDRWFMRWLKPYIDFVPLDPTKPLAIKGLIKVIERGQPVVVFPEGRISVTGSLMKVYSGAAFVAAKSGATIIPVRIDGIELSPFGRLAGVFKRRCLPQVTITYLPPTTLPMPEASSARARRALAGERLHQIMMKARMETRPQHTLYQAFLAARSRYGRHSASIADISFNEDSYQGLLKKSLGVSRILQRFTRADEHVGMLLPNATITAASILGASLRNRIPAMLNYTAGAKGLQSAMKAAGIKTIVTSRQFLEKGKLTDLPKQVSEANWVYLEDLKDTVTLKDKLWILFHLLFPARAMLPQKPDDAAIVLFTSGSEGNPKGVVHSHDSLLANVEQIRTVADFTPGDRFMSALPLFHAFGLTVGLLTPLITGARVFLYPSPLHYRIVPELVYDQNCTVLFGTSTFLGNYARFAHPYDFARLRYVVAGAEKLSETTRQVWQDKFGIRILEGYGVTECAPVVAINVPMATKIHSVGLLLPEMESRLITVPGITRGGRLQLRGPNIMKGYLRVENPGVLETPAAENAEGELQQGWYDTGDIVELDERGFCTIIGRVKRFAKLAGEMVSLESVEQLAVKVSPEAQHAASAKSDSSKGEALVLFTTDSQITRDVLLAQARSSGVPELAVPRDIRYVKALPLLGSGKPDFVTLRQMAEEPNSEQSVIEPSIVKQPITNASEPSA

Gene
aas
Protein
Bifunctional protein Aas
Organism
Pectobacterium carotovorum subsp. carotovorum (strain PC1)
Length
723 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
79.996 kDa
Sequence
MIHTLLRWVFQRLYRIRIEGDSSQFQQSKLLITPNHVSFLDGILLALFLPIKPVFAVYSSISDRWFMRWLKPYIDFVPLDPTKPLAIKGLIKVIERGQPVVVFPEGRISVTGSLMKIYSGAAFVAAKSGATIIPVRIDGAEFTPFGRLAGVFKRRCFPQITITYLPPTTLPMPEADSARTRRALAGEHLHQIMMKARMETRPQHTLYEAFLAARTRYGRRSPSIADISFNEDSYQGLLKKSLGVSRILQRFTRADEHVGMLLPNATITAASILGASLRNRIPAMLNYTAGAKGLQSAMKAAGIKTIVTSRQFLEKGKLTDLPKQVSEANWVYLEDLKDTVTLADKLWILFHLLFPARAMLPQKPDDAAIVLFTSGSEGNPKGVVHSHDSLLANVEQIRTVADFTPRDRFMSALPLFHAFGLTVGLLTPLMTGARIFLYPSPLHYRIVPELVYDQNCTVLFGTSTFLGNYARFAHPYDFARLRYVVAGAEKLSETTRQVWQDKFGIRILEGYGVTECAPVVAINVPMATKIHSVGLLLPEIESRLITVPGITRGGRLQLRGPNIMKGYLRVENPGVLEAPAAENAEGELQQGWYDTGDIVELDEKGFCTIIGRVKRFAKLAGEMVSLESVEQLAVKVSPEAQHAASAKSDSSKGEALVLFTTDSQITRDVLLAQARSSGVPELAVPRDIRYVKALPLLGSGKPDFVTLRHMAEEPVTNASEQSA

Gene
aas
Protein
Bifunctional protein Aas
Organism
Escherichia coli O7:K1 (strain IAI39 / ExPEC)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.752 kDa
Sequence
MLFSFFRNLCRVLYRVRVTGDNQALKGERVLITPNHVSFIDGILLALFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVQMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGSSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Escherichia coli (strain K12 / MC4100 / BW2952)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.7 kDa
Sequence
MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVAMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRMPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Escherichia coli (strain K12 / DH10B)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.7 kDa
Sequence
MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVAMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRMPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Escherichia coli O9:H4 (strain HS)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.682 kDa
Sequence
MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVAMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Escherichia coli O1:K1 / APEC
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.826 kDa
Sequence
MLFSFFRNLCRVLYRVRVTGDTKALKGERVLITPNHVSFIDGILLALFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVEMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENIRGEMERDWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Escherichia coli O6:K15:H31 (strain 536 / UPEC)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.842 kDa
Sequence
MLFSFFRNLCRVLYRVRVTGDTKALKGERVLITPNHVSFIDGILLALFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVEMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERDWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELMRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.768 kDa
Sequence
MLFSFFRNLCRVLYRVRVTGDTKALKGERVLITPNHVSFIDGILLALFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVEMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQLKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.682 kDa
Sequence
MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVAMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Escherichia coli (strain K12)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.7 kDa
Sequence
MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVAMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRMPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.784 kDa
Sequence
MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLALFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVEMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSIEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFSHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Escherichia coli (strain SE11)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.74 kDa
Sequence
MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVEMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Escherichia coli (strain SMS-3-5 / SECEC)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.735 kDa
Sequence
MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLALFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVEMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGEHIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Escherichia coli (strain UTI89 / UPEC)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.826 kDa
Sequence
MLFSFFRNLCRVLYRVRVTGDTKALKGERVLITPNHVSFIDGILLALFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVEMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENIRGEMERDWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Enterobacter sp. (strain 638)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.333 kDa
Sequence
MLFGFFRTLFRILFRIRLTGDTQSLQGERVLITPNHVSFIDGILLALFLPGRPVFAVYSSISQKWFMRWLAPLVDLVPLDPTKPMMIKHLVRLIEQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSKATVVPLRIEGAELTYFSRLKGLVKQRLFPQITLHILPPTTLPMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYEALLSAQDRYGARKNCVEDINFTPDTYRKLLTKTLFVGRILEKYSQKGEKIGLMLPNAGISAAVIFGAVSRGRIPAMMNYTAGVKGLTSAITAAEIKTVFTSRQFLDKGKLWHLPEQLKQVRWVFLEDLKAEVTTADKLWIFAHLLVPHLAQVKQQPEDAAMILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTAKDRFMSALPLFHSFGLTVGLFTPLFTGAEVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLGHYARFANPYDFFRVRYVVAGAEKLQDSTREIWQDKFGLRILEGYGVTECAPVVSINVPMAARPGTVGRILPGMDARLLAVPGIEEGGRLQLKGPNVMNGYLRVENPGVLEAPTAENAAGEVETGWYDTGDIVRFDEHGFVQIQGRAKRFAKIAGEMVSLEMVEQLANALSPEKMHATAIKSDASKGEALVLFTTDSELKREQLLHYAREHGVPELAVPRDIRYLKQLPVLGSGKPDFVALKSMVEEEEHHDA

Gene
aas
Protein
Bifunctional protein Aas
Organism
Erwinia tasmaniensis (strain DSM 17950 / CIP 109463 / Et1/99)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
79.917 kDa
Sequence
MVLTFLRALLRLAFRTRLTGDLASLNKRRVLITPNHMSFLDGILLAVFLPVKPVFAVYSSISSQWYMRALRSLIDFVPLDPTKPMSVKHLVKLIGQGRPVVIFPEGRITVTGSLMKIYDGAGFVAAKSQATVVPLRIEGAEYTPFGRLGGVVKRRLFPRITLTVLPATTIPMPQAPRARDRRRLAGEHLHHIMMEARMAVRPRETLYQAFLAARTRYGLFKPCIEDVNFKPDSYSGLLKKSLGVGRILERYSQPGEYVGLLLPNATVTAAAILGASMRGRVPAMLNYTAGVKGLTSALTAGEIKTVFTSRQFLDKGKLWHLPQGITQVKWIYLEDLKDTLTTQDKLWILGHLLLPRRAMVAQQPEDAAMVLFTSGSEGHPKGVVHSHKSLLANVEQIRTVADFTPCDRFMSALPLFHAFGLTVGLFTPLMTGARVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFARLRYVVAGAEKLQDHTRELWMEKYGIRILEGYGVTECAPVVAINVPMAAKSHTVGRILPGMDSRLVSVPGIEQGGRLQLRGPNIMKGYLRVEHPGRLEAPQADNGEGQMEPGWYDTGDIVSFDEGGFCQIQGRVKRFAKIAGEMVSLEIVEQIARNASDDKQHAATIKPDGNRGEALVLFTTDAQLTREQLMHSARELGSPELAVPRDIRLLSQLPLLGSGKPDFVTLREMAEQPEDRRE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.488 kDa
Sequence
MLFGFFRKLCQVLYRVQVTGDPAALKGERVLITPNHVSFIDGILLALFLPVRPVFAVYTSISQQWYMRWLQSLIDFVPLDPTKPMAIKHLVRLVEQGRPVVIFPEGRITVTGSLMKIYDGAGFVAAKSGATVVPVRIEGAELTHFSRLKGLVKRRLFPKIHLHILPPTHVPMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLGAMHRYGGGKNCVEDVNFTPDSYRKLLTKTLFVGRILEKYSAEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWIYLEDLKADVTLTDKVWIFAHLLMPHLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLAVPGIEDGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENIQGELERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDSELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEPEKHNE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Klebsiella pneumoniae (strain 342)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.274 kDa
Sequence
MLLGFFRLLFKGLYRVRLTGDTQALYQQKVLITPNHVSFLDGILLALFLPVRPVFAVYTSISQRWFMRALTPIIDFVPLDPTKPMSIKHLVRLIEQGRPVVIFPEGRISVSGSLMKIYDGAAFVAAKSQATIVPLRIDGAELTPFSRLKGLVKRRLFPRIQLHLLPPTHLPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAQDRFGARKPCVEDINFQPDTYRKLLTKTLFVARILEKYSQRGEKIGLMLPNAGISAAVIFGAIARGRIPAMMNYTAGVKGLSSAIAAAEINTIFTSRTFLDKGKLWHLPEQLTQVRWVFLEDLKGDITLADKLWIFGHLLAPRLAQVKQQPEDAAMILFTSGSEGNPKGVVHSHKSLLANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLLTPLFTGAEVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLANYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKVGTVGRILPGMDARLLAMPGIEQGGRLQLKGPNIMKGYLRVENPGVLEAPAAENQHGEKEAGWYDTGDIVTFDEQGYVRIQGRAKRFAKIAGEMISLEMVEQVALGASPDKMHATAIKQDASKGEALVLFTTDNELTREALLRYARQHGVPELAVPRDIRWLKQLPVLGSGKPDYVTLKNMVDEAETTHE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.214 kDa
Sequence
MLLGFFRLLFKGLYRVRLTGDTQALYQQKVLITPNHVSFLDGILLALFLPVRPVFAVYTSISQRWFMRALTPIIDFVPLDPTKPMSIKHLVRLIEQGRPVVIFPEGRISVSGSLMKIYDGAAFVAAKSQATIVPLRIEGAELTPFSRLKGLVKRRLFPRIQLHLLPPTHLPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAQDRFGARKPCVEDINFQPDTYRKLLTKTLFVARILEKYSQPGEKIGLMLPNAGISAAVIFGAIARGRIPAMMNYTAGVKGLSSAIAAAELNTIFTSRTFLDKGKLWHLPEQLTQVRWVFLEDLKGDITLADKLWIFAHLLAPRLAQVKQQPEDAAMILFTSGSEGNPKGVVHSHKSLLSNVEQIKTIADFTANDRFMSALPLFHSFGLTVGLLTPLLTGAEVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLANYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKVGTVGRILPGMDARLLAMPGIDQGGRLQLKGPNIMKGYLRVENPGVLEAPAAENQHGEMEAGWYDTGDIVTFDEQGYVRIQGRAKRFAKIAGEMISLEMVEQVALGASPDKMHATAIKQDASKGEALVLFTTDNELTREALLRYARQHGVPELAVPRDIRWLKQLPVLGSGKPDYVTLKNMVDEAETTHE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.223 kDa
Sequence
MLFGFFRNLFRVLYRVRVTGDARALQGERILITPNHVSFIDGILLALFLPVRPVFAVYSSISQQWYMRWLKSLIDFVPLDPTKPMAIKHLVRLVEQGRPVVIFPEGRISVSGSLMKIYDGAGFVAAKSGATVVPVRIEGAELTHFSRLKGLVKQRFFPRIHLHILPPTHLPMPEAPRARERRKLAGEMLHQIMMEARMAVRPRETLYESLLAAQYRYGAGKNCVEDINFTPDTYRKLLTKTLFVGRILEKYSAQGENIGLMLPNAAISAAVIFGAVSRGRIPAMMNYTAGVKGLTSAITAAEIKTVFTSRQFLEKGKLWHLPEQLTQVRWIYLEDLKADVTLADKLWIFAHLLMPRLAQVKQRPEEAAMILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLLTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFYRLRYVVAGAEKLQDSTRQLWQDKFGLRVLEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLAVPGIDDGGRLQLKGPNIMNGYLRVEKPGVLEAPAAENALGDVEQGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKMHATAIKSDASKGEALVLFTTDGELTRESLLQYARTHGIPELAVPRDIRYLKQLPLLGSGKPDFVTLKSWVDEPEKQHA

Gene
aas
Protein
Bifunctional protein Aas
Organism
Cronobacter sakazakii (strain ATCC BAA-894)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
79.978 kDa
Sequence
MVLKFFRWLFRLLFRIQVYGDTGPLTQQRVLITPNHVSFLDGALMALFLPVRPVFAVYTSISQQWYMRALKPLIDFVPLDPTKPMSVKQLVRLVGEGRPVVIFPEGRISISGSLMKIYEGAGFVAAKSQATVIPVRIEGAELTFFSRLKGLVKRRLFPRISIHILPPTSIPMPDAPKARDRRKMAGEMLHQVMMEARMAARPRETLFEALINAQKRYGESKSCLEDINFKPDTYRSLMMKTLFVGRILDKYSAPREAIGLMLPNASISAAVIFGAVMRGRIPAMMNYTAGVQGLTSAITAAQIKTIFTSRQFLDKGKLWHLSEQITSVRWVFLEDLKGEVTAKDKAWIFAHLLMPRLAQVEQQPEDAALILFTSGSEGNPKGVVHSHKSLLANVEQIRTIADFTADDKFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRVVPELVYDRNCTVIFGTSTFLGHYARFAHPYDFHLVRYVVAGAEKLQESTKQIWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPAMDARLVEVPGIEQGGRLQLKGPNIMKGYLRVENPGVLEAPAAENPQGVSEPGWYDTGDIVAFDEQGFVQIQGRAKRFAKIAGEMVSLEMVESLALAVSPEKMHATAIKHDAAKGEALVLFTTDPELTREKLAQQARSKGVPELAVPRDIRFLKQLPLLGSGKPDFVSLKKLVDQEETHHA

Gene
aas
Protein
Bifunctional protein Aas
Organism
Escherichia coli O139:H28 (strain E24377A / ETEC)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.682 kDa
Sequence
MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVAMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Escherichia coli O127:H6 (strain E2348/69 / EPEC)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.768 kDa
Sequence
MLFSFFRNLCRVLYRVRVTGDTKALKGERVLITPNHVSFIDGILLALFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVEMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQLKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Escherichia coli O45:K1 (strain S88 / ExPEC)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.826 kDa
Sequence
MLFSFFRNLCRVLYRVRVTGDTKALKGERVLITPNHVSFIDGILLALFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVEMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENIRGEMERDWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Escherichia coli (strain 55989 / EAEC)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.74 kDa
Sequence
MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVEMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Escherichia coli O157:H7
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.764 kDa
Sequence
MLFSFFRNLCRVLYRVRVTGDPQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVEMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEVEQHDE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Escherichia coli O157:H7 (strain EC4115 / EHEC)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.764 kDa
Sequence
MLFSFFRNLCRVLYRVRVTGDPQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVEMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEVEQHDE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Salmonella agona (strain SL483)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.492 kDa
Sequence
MLFGFFRNLFRVLYRVRVTGDVRALQGNRVLITPNHVSFIDGMLLALFLPVRPVFAVYTSISQQWYMRWLTPLIDFVPLDPTKPMSIKHLVRLVEQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSGATVIPLRIDGAELTPFSRLKGLVKRRLFPRIQLHILPPTQIPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAQYRYGAGKNCIEDINFTPDTYRKLLTKTLFVGRILEKYSVKGEKIGLMLPNAAISAAVIFGAVSRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTPADKLWIFAHLLAPRLAQVKQQPEDAAIILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLAVPGIENGGRLQLKGPNIMNGYLRVEKPGVLEVPSAENARGETERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSADKMHATAIKSDASKGEALVLFTTDSELTREKLQHYAREHGIPELAVPRDIRYLKQLPLLGSGKPDFVTLKSWVDAPEQHHE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Salmonella choleraesuis (strain SC-B67)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.537 kDa
Sequence
MLFGFFRNLFRVLYRVRVTGDVQALQGNRVLITPNHVSFIDGMLLALFLPVRPVFAVYTSISQQWYMRWLTPLIDFVPLDPTKPMSIKHLVRLVEQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSGATVIPLRIDGAELTPFSRLKGLVKRRLFPRIQLHILPPTQIPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAQYRYGAGKNCIEDINFTPDTYRKLLTKTLFVGRILEKYSVEGEKIGLMLPNAAISAAVIFGAVSRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTPADKLWIFAHLLAPRLAQVKQQPEDEAIILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLAVPGIENGGRLQLKGPNIMNGYLRVEKPGVLEVPSAENARGETERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSAEKMHATAIKSDASKGEALVLFTTDSELTREKLQHYAREHGIPELAVPRDIRYLKQLPLLGSGKPDFVTLKSWVDAPEQHHE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Salmonella dublin (strain CT_02021853)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.523 kDa
Sequence
MLFGFFRNLFRVLYRVRVTGDVRALQGNRVLITPNHVSFIDGMLLALFLPVRPVFAVYTSISQQWYMRWLTPLIDFVPLDPTKPMSIKHLVRLVVQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSGATVIPLRIDGAELTPFSRLKGLVKRRLFPRIQLHILPPTQIPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAQYRYGAGKNCIEDINFTPDTYRKLLTKTLFVGRILEKYSVEGEKIGLMLPNAAISAAVIFGAVSRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTLADKMWIFAHLLAPRLAQVKQQPEDAAIILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVLINVPMAAKPGTVGRILPGMDARLLAVPGIENGGRLQLKGPNIMNGYLRVEKPGVLEVPSAENARGETERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSADKMHATAIKSDASKGEALVLFTTDSELTREKLQHYAREHGIPELAVPRDIRYLKQLPLLGSGKPDFVTLKSWVDAPEQHHE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Salmonella enteritidis PT4 (strain P125109)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.493 kDa
Sequence
MLFGFFRNLFRVLYRVRVTGDVRALQGNRVLITPNHVSFIDGMLLALFLPVRPVFAVYTSISQQWYMRWLTPLIDFVPLDPTKPMSIKHLVRLVEQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSGATVIPLRIDGAELTPFSRLKGLVKRRLFPRIQLHILPPTQIPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAQYRYGAGKNCIEDINFTPDTYRKLLTKTLFVGRILEKYSVEGEKIGLMLPNAAISAAVIFGAVSRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTPADKLWIFAHLLAPRLAQVKQQPEDAAIILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLAVPGIENGGRLQLKGPNIMNGYLRVEKPGVLEVPSAENARGETERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSADKMHATAIKSDASKGEALVLFTTDSELTREKLQHYAREHGIPELAVPRDIRYLKQLPLLGSGKPDFVTLKSWVDAPEQHHE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Salmonella gallinarum (strain 287/91 / NCTC 13346)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.467 kDa
Sequence
MLFGFFRNLFRVLYRVRVTGDVRALQGNRVLITPNHVSFIDGMLLALFLPVRPVFAVYTSISQQWYMRWLTPLIDFVPLDPTKPMSIKHLVRLVEQGRAVVIFPEGRISVTGSLMKIYDGAGFVAAKSGATVIPLRIDGAELTPFSRLKGLVKRRLFPRIQLHILPPTQIPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAQYRYGAGKNCIEDINFTPDTYRKLLTKTLFVGRILEKYSVEGEKIGLMLPNAAISAAVIFGAVSRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTPADKLWIFAHLLAPRLAQVKQQPEDAAIILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLAVPGIENGGRLQLKGPNIMNGYLRVEKPGVLEVPSAENARGETERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSADKMHATAIKSDASKGEALVLFTTDSELTREKLQHYAREHGIPELAVPRDIRYLKQLPLLGSGKPDFVTLKSWVDAPEQHHE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Salmonella heidelberg (strain SL476)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.493 kDa
Sequence
MLFGFFRNLFRVLYRVRVTGDVRALQGNRVLITPNHVSFIDGMLLALFLPVRPVFAVYTSISQQWYMRWLTPLIDFVPLDPTKPMSIKHLVRLVEQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSGATVIPLRIDGAELTPFSRLKGLVKRRLFPRIQLHILPPTQIPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAQYRYGAGKNCIEDINFTPDTYRKLLTKTLFVGRILEKYSVEGEKIGLMLPNAAISAAVIFGAVSRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTPADKLWIFAHLLAPRLAQVKQQPEDAAIILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLAVPGIENGGRLQLKGPNIMNGYLRVEKPGVLEVPSAENARGETERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSADKMHATAIKSDASKGEALVLFTTDSELTREKLQHYAREHGIPELAVPRDIRYLKQLPLLGSGKPDFVTLKSWVDAPEQHHE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Salmonella newport (strain SL254)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.527 kDa
Sequence
MLFGFFRNLFRVLYRVRVTGDVRVLQGNRVLITPNHVSFIDGMLLALFLPVRPVFAVYTSISQQWYMRWLTPLIDFVPLDPTKPMSIKHLVRLVEQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSGATVIPLRIDGAELTPFSRLKGLVKRRLFPRIQLHILPSTQIPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAQYRYGAGKNCIEDINFTPDTYRKLLTKTLFVGRILEKYSVEGEKIGLMLPNAAISAAVIFGAVSRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTPADKLWIFAHLLAPRLAQVKQQPEDAAIILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLAVPGIENGGRLQLKGPNIMNGYLRVEKPGVLEVPSAENSRGETERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSADKMHATAIKSDASKGEALVLFTTDSELTREKLQHYAREHGIPELAVPRDIRYLKQLPLLGSGKPDFVTLKSWVDAPEQHHE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Salmonella paratyphi A (strain ATCC 9150 / SARB42)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.511 kDa
Sequence
MLFGFFRNLFRVLYRVRVTGDVRALQGNRVLITPNHVSFIDGMLLALFLPVRPVFAVYTSISQQWYMRWLTPLIDFVPLDPTKPMSIKHLMRLVEQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSGATVIPLRIDGAELTPFSRLKGLVKRRLFPRIQLHILPPTQIPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAQYRYGAGKNCIEDINFTPDTYRKLLTKTLFVGRILEKYSVEGEKIGLMLPNAAISAAVIFGAVSRRRIPAMMNYTAGVKGLTSAIAAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTLADKLWIFAHLLAPRLAQVKQQPEDAAIILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLAVPGIENGGRLQLKGPNIMNGYLRVEKPGVLEVPSAENARGETERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSADKMHATAIKSDASKGEALVLFTTDSELTREKLQHYAREHGIPELAVPRDIRYLKQLPLLGSGKPDFVTLKSWVDAPEQHHE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.521 kDa
Sequence
MLFGFFRNLFRVLYRVRVTGDVRALQGNRVLITPNHVSFIDGMLLALFLPVRPVFAVYTSISQQWYMRWLTPLIDFVPLDPTKPMSIKHLVRLVEQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSGATVIPLRIDGAELTPFSRLKGLVKRRLFPRIQLHILPPTQIPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLVAQYRYGAGKNCIEDINFTPDTYRKLLTKTLFVGRILEKYSVEGEKIGLMLPNAAISAAVIFGAVSRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTPADKLWIFAHLLAPRLAQVKQQPEDAAIILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLAVPGIENGGRLQLKGPNIMNGYLRVEKPGVLEVPSAENARGETERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSADKMHATAIKSDASKGEALVLFTTDSELTREKLQHYAREHGIPELAVPRDIRYLKQLPLLGSGKPDFVTLKSWVDAPEQHHE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Salmonella paratyphi C (strain RKS4594)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.537 kDa
Sequence
MLFGFFRNLFRVLYRVRVTGDVQALQGNRVLITPNHVSFIDGMLLALFLPVRPVFAVYTSISQQWYMRWLTPLIDFVPLDPTKPMSIKHLVRLVEQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSGATVIPLRIDGAELTPFSRLKGLVKRRLFPRIQLHILPPTQIPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAQYRYGAGKNCIEDINFTPDTYRKLLTKTLFVGRILEKYSVEGEKIGLMLPNAAISAAVIFGAVSRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTPADKLWIFAHLLAPRLAQVKQQPEDEAIILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLAVPGIENGGRLQLKGPNIMNGYLRVEKPGVLEVPSAENARGETERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSAEKMHATAIKSDASKGEALVLFTTDSELTREKLQHYAREHGIPELAVPRDIRYLKQLPLLGSGKPDFVTLKSWVDAPEQHHE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Salmonella paratyphi A (strain AKU_12601)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.511 kDa
Sequence
MLFGFFRNLFRVLYRVRVTGDVRALQGNRVLITPNHVSFIDGMLLALFLPVRPVFAVYTSISQQWYMRWLTPLIDFVPLDPTKPMSIKHLMRLVEQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSGATVIPLRIDGAELTPFSRLKGLVKRRLFPRIQLHILPPTQIPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAQYRYGAGKNCIEDINFTPDTYRKLLTKTLFVGRILEKYSVEGEKIGLMLPNAAISAAVIFGAVSRRRIPAMMNYTAGVKGLTSAIAAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTLADKLWIFAHLLAPRLAQVKQQPEDAAIILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLAVPGIENGGRLQLKGPNIMNGYLRVEKPGVLEVPSAENARGETERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSADKMHATAIKSDASKGEALVLFTTDSELTREKLQHYAREHGIPELAVPRDIRYLKQLPLLGSGKPDFVTLKSWVDAPEQHHE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Salmonella schwarzengrund (strain CVM19633)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.52 kDa
Sequence
MLFGFFRNLFRVLYRVRVTGDVRALQGNRVLITPNHVSFIDGMLLALFLPVRPVFAVYTSISQQWYMRWLTPLIDFVPLDPTKPMSIKHLVRLVEQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSGATVIPLRIDGAELTPFSRLKGLVKRRLFPRIQLHILPPTQIPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAQYRYGAGKNCIEDINFTPDTYRKLLTKKLFVGRILEKYSVEGEKIGLMLPNAAISAAVIFGAVSRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTPADKLWIFAHLLAPRLAQVKQQPEDAAIILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLAVPGIENGGRLQLKGPNIMNGYLRVEKPGVLEVPSAENARGETERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSADKMHATAIKSDASKGEALVLFTTDSELTREKLQHYAREHGIPELAVPRDIRYLKQLPLLGSGKPDFVTLKSWVDAPEQHHE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Salmonella typhi
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.477 kDa
Sequence
MLFGFFRNLFRVLYRVRVTGDVRALQGNRVLIAPNHVSFIDGMLLALFLPVRPVFAVYTSISQQWYMRWLTPLIDFVPLDPTKPMSIKHLVRLVEQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSGATVIPLRIDGAELTPFSRLKGLVKRRLFPRIQLHILPPTQIPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAQYRYGAGKNCIEDINFTPDTYRKLLTKTLFVGRILEKYSVEGEKIGLMLPNAAISAAVIFGAVSRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTPADKLWIFAHLLAPRLAQVKQQPEDAAIILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLAVPGIENGGRLQLKGPNIMNGYLRVEKPGVLEVPSAENARGETERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSAEKMHATAIKSDASKGEALVLFTTDSELTREKLQHYAREHGIPELAVPRDIRYLKQLPLLGSGKPDFVTLKSWVDAPEQHHE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.509 kDa
Sequence
MLFGFFRNLFRVLYRVRVTGDVRALQGNRVLITPNHVSFIDGMLLALFLPVRPVFAVYTSISQQWYMRWLTPLIDFVPLDPTKPMSIKHLVRLVEQGRPVVIFPEGRISVTGSLMKIYDGAGFVAAKSGATVIPLRIDGAELTPFSRLKGLVKRRLFPRIQLHILPPTQIPMPEAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLAAQYRYGAGKNCIEDINFTPDTYRKLLTKTLFVGRILEKYSVEGEKIGLMLPNAAISAAVIFGAVSRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTPADKLWIFAHLLAPRLAQVKQQPEDAAIILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTANDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLAVPGIENGGRLQLKGPNIMNGYLRVEKPGVLEVPSAENSRGETERGWYDTGDIVRFDENGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSADKMHATAIKSDASKGEALVLFTTDSELTREKLQHYAREHGIPELAVPRDIRYLKQLPLLGSGKPDFVTLKSWVDAPEQHHE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Shigella boydii serotype 18 (strain CDC 3083-94 / BS512)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.686 kDa
Sequence
MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVAMPDASRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWIDEAEQHDE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Shigella flexneri serotype 5b (strain 8401)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.668 kDa
Sequence
MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVAMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPDLVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Shigella flexneri
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.668 kDa
Sequence
MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVAMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPDLVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Shigella sonnei (strain Ss046)
Length
719 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
80.74 kDa
Sequence
MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVEMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE

Gene
aas
Protein
Bifunctional protein Aas
Organism
Yersinia pseudotuberculosis serotype O:1b (strain IP 31758)
Length
718 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
79.416 kDa
Sequence
MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTHLPEQVNEVNWVYLEDLKDTVTLTDKLWILFHLCFPRRAMLPQQADDSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVPGIAQGGRLQLRGPNIMRGYLRVENPGVLEQPSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFTTDSEITRERLIKAARENGVPELAVPRDIRVVKALPLLGSGKPDFVTLGKMAQDPEMSV

Gene
aas
Protein
Bifunctional protein Aas
Organism
Yersinia pestis bv. Antiqua (strain Antiqua)
Length
718 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
79.386 kDa
Sequence
MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTHLPEQVNEVNWVYLEDLKDTVTLTDKLWILFHLCFPRRAMLPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVPGIAQGGRLQLRGPNIMRGYLRVENPGVLEQPSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFTTDSEITRERLIKVARENGVPELAVPRDIRVVKALPLLGSGKPDFVTLGKMAQDPEMSV

Gene
aas
Protein
Bifunctional protein Aas
Organism
Yersinia pseudotuberculosis serotype IB (strain PB1/+)
Length
718 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
79.416 kDa
Sequence
MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTHLPEQVNEVNWVYLEDLKDTVTLTDKLWILFHLCFPRRAMLPQQADDSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVPGIAQGGRLQLRGPNIMRGYLRVENPGVLEQPSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFTTDSEITRERLIKAARENGVPELAVPRDIRVVKALPLLGSGKPDFVTLGKMAQDPEMSV

Gene
aas
Protein
Bifunctional protein Aas
Organism
Yersinia pestis
Length
718 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
79.386 kDa
Sequence
MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTHLPEQVNEVNWVYLEDLKDTVTLTDKLWILFHLCFPRRAMLPQQADGSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVPGIAQGGRLQLRGPNIMRGYLRVENPGVLEQPSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFTTDSEITRERLIKVARENGVPELAVPRDIRVVKALPLLGSGKPDFVTLGKMAQDPEMSV

Gene
aas
Protein
Bifunctional protein Aas
Organism
Yersinia pestis bv. Antiqua (strain Angola)
Length
718 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
79.445 kDa
Sequence
MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTHLPEQVNEVNWVYLEDLKDTVTLTDKLWILFHLCFPRRAMLPQQADDSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVPGIAQGGRLQLRGPNIMRGYLRVENPGVLEQPSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFTTDSEITRERLIKVARENGVPELAVPRDIRVVKALPLLGSGKPDFVTLGKMAQDPEMSV

Gene
aas
Protein
Bifunctional protein Aas
Organism
Yersinia pestis (strain Pestoides F)
Length
718 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
79.445 kDa
Sequence
MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTHLPEQVNEVNWVYLEDLKDTVTLTDKLWILFHLCFPRRAMLPQQADDSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVPGIAQGGRLQLRGPNIMRGYLRVENPGVLEQPSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFTTDSEITRERLIKVARENGVPELAVPRDIRVVKALPLLGSGKPDFVTLGKMAQDPEMSV

Gene
aas
Protein
Bifunctional protein Aas
Organism
Yersinia pseudotuberculosis serotype I (strain IP32953)
Length
718 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
79.416 kDa
Sequence
MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTHLPEQVNEVNWVYLEDLKDTVTLTDKLWILFHLCFPRRAMLPQQADDSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVPGIAQGGRLQLRGPNIMRGYLRVENPGVLEQPSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFTTDSEITRERLIKAARENGVPELAVPRDIRVVKALPLLGSGKPDFVTLGKMAQDPEMSV

Gene
aas
Protein
Bifunctional protein Aas
Organism
Yersinia pseudotuberculosis serotype O:3 (strain YPIII)
Length
718 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
79.416 kDa
Sequence
MAYRLLRALFRGLFRVTIDGVTDQFKHEKLIITPNHVSFLDGALLALFLPIKPVFAVYTSITDTWYMRWLKPYVDFVALDPTNPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLDGPEFTHFGRLQGVLKTRWFPKISIHVLPATTIPMPQAPRSRERRVLAGEHLHTIMMAARMATVPRETLFEALLSAQTRYGRFKPCIEDVSFKEDSYQTLLKKTLGVSRILQRFTVPGEHVGMLLPNATITAAAIFGASLRGRIPALLNYTSGAKGLQSAIIAASLKTIVTSRQFLEKGKLTHLPEQVNEVNWVYLEDLKDTVTLTDKLWILFHLCFPRRAMLPQQADDSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFARVRYVVAGAEKLAESTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMEARLINVPGIAQGGRLQLRGPNIMRGYLRVENPGVLEQPSAENAQGELDANWYDTGDIVTLDEQGFCAIRGRVKRFAKLAGEMVSLESVEQLAISLSPEGQHAAAAKTDSAKGEALVLFTTDSEITRERLIKAARENGVPELAVPRDIRVVKALPLLGSGKPDFVTLGKMAQDPEMSV

Gene
aas
Protein
Bifunctional protein Aas
Organism
Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)
Length
718 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
79.473 kDa
Sequence
MAYRLLRALFRGLFRVTIDGITDQFSHQKLIITPNHVSFLDGALLALFLPIKPVFAVYSNITESWYMRWLKPYVDFVALDPTKPMAIKHLVRMVEQGRPVVIFPEGRITVTGSLMKIYDGAAFVAAKSGAAVVPIRLEGPEFTRFGRLGDVLKVRWFPKISIHVLPATTLPMPQAPRARDRRVLAGERLHAIMMAARMAIVPRETLFEALLSAQTRYGRFKPCIEDISFKEDSYQTLLKKILGVSRILQRFTAQGEHVGMLLPNATITAAAIFGATLRGRIPALLNYTSGAKGLKSAITAASLKTIITSRQFLEKGKLTHLPEQVTEANWVYLEDLKDTVTLADKLWILFHLCCPRRAMVPQQADDSALILFTSGSEGNPKGVVHSHASLLANVEQIRTIADFTPRDRFMSSLPLFHAFGLTVGLFTPLMTGSRVFLYPSPLHYRVVPELVYDRNCTVLFGTSTFLGNYARFAHPYDFARLRYVVAGAEKLADSTKQIWQDKFGIRILEGYGVTECAPVVAINVPMAAKVNTVGRILPGMESRVIPVPGIEQGGRLQLRGPNIMRGYLRVEKPGVLEQPSAENTQGEQEAGWYDTGDIVAIDEQGFCTIRGRMKRFAKLAGEMVSLESVEQLVLRISPEGQHAAATKTDSAKGEALVLFTTDSEITREKLVKAARESGVPELAVPRDIRVVKALPLLGSGKPDFVTLSKMAEDPEMSA

Gene
aas
Protein
Bifunctional protein Aas
Organism
Photorhabdus luminescens subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01)
Length
639 amino acids
Function
Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1.
Similarity
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Mass
71.809 kDa
Sequence
MLFKFLRLVFRLMFRLTVEGDIKQFNHPKCLITPNHVSFLDGVLLTLFLPVKPVFAVYSNIANRGFMKLVSRYVEIVPLDPINPMAVRILVKEIEKGRPIVVFPEGRITVTGSLMKIYDGAAFIAAISEAVVVPVRFEGLERTLFSRLKGIFKLHLFPKVTMKILPATQLLMPNASSSEQRRRLAGERLHEIMMNARMATRPQETIFESLLVARKQFGRFKPCIEDVSFKEDSYNSLLKKVLAASRILQRFTCQGERIGFLLPNATIMVAAIFGASLRGRIPALLNYTTDSHGLKNALAVASIKTIVTSRQFLKKERLTHLSEQVTEVNWVYLEDLESTVTLLDKLWILWHLFFPKQAMVAQKPDDDALVLFTSGSDAVSKGVVHSHASLLANVEQIKTITDFNPLDRFMSSLPLFHAFGLTVGLFTPLLSGSRIFLYPNPLHYRVVPELVYECNCTVLLGTSSFLENYAYSAHPYDFARLRCVIAGIEKLAENTKQIWQDKFGIRILEGYGMTECAPVIALNVPMMAKVGTVGRILPAMEFRLIPIAGIKQGGRLQLRGPNMMKGYLRMEDPNHLEPPAVKDEHGNIQFDWLDTGDIVSIDEQGFCTILGRGKRFAKQGELDGGKADFVTLCKIAEAE