B5Z4F4 · AAS_ECO5E
- ProteinBifunctional protein Aas
- Geneaas
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids719 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
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.
Catalytic activity
- a 2-acyl-sn-glycero-3-phosphoethanolamine + a fatty acyl-[ACP] = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + holo-[ACP]
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 36 | |||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase activity | |
Molecular Function | ATP binding | |
Molecular Function | long-chain fatty acid [acyl-carrier-protein] ligase activity | |
Molecular Function | medium-chain fatty acid-CoA ligase activity | |
Biological Process | fatty acid metabolic process | |
Biological Process | phospholipid biosynthetic process |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameBifunctional protein Aas
Including 2 domains:
- Recommended name2-acylglycerophosphoethanolamine acyltransferase
- EC number
- Alternative names
- Recommended nameAcyl-[acyl-carrier-protein] synthetase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionB5Z4F4
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 258-277 | Helical | ||||
Sequence: IGLMLPNAGISAAVIFGAIA | ||||||
Transmembrane | 409-433 | Helical | ||||
Sequence: FMSALPLFHSFGLTVGLFTPLLTGA |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000137886 | 1-719 | Bifunctional protein Aas | |||
Sequence: MLFSFFRNLCRVLYRVRVTGDPQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVEMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEVEQHDE |
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 15-138 | Acyltransferase | ||||
Sequence: RVRVTGDPQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIE | ||||||
Region | 233-646 | AMP-binding | ||||
Sequence: SYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAI |
Sequence similarities
In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family.
In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length719
- Mass (Da)80,764
- Last updated2008-11-25 v1
- Checksum786640F7D3330B7C
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001164 EMBL· GenBank· DDBJ | ACI38434.1 EMBL· GenBank· DDBJ | Genomic DNA |