P31119 · AAS_ECOLI
- ProteinBifunctional protein Aas
- Geneaas
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids719 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 | membrane | |
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 | long-chain fatty acid-CoA ligase activity | |
Biological Process | fatty acid metabolic process | |
Biological Process | phospholipid biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
The enzyme catalyzes transfer of an acyl chain to the headgroup of phosphatidylethanolamine (PE) and phosphatidylglycerol (PG), generating N-acylphosphatidylamine or headgroup acylated phosphatidylglycerol. Over-expression of the gene increases levels of these PLs (phospholipids) to 15% and 25%, respectively. KO abolishes these lipid classes.
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
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP31119
- Secondary accessions
Proteomes
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
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 36 | Loss of 2-acyl-GPE acyltransferase activity; retains acyl-ACP synthetase activity. | ||||
Sequence: H → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000193046 | 1-719 | Bifunctional protein Aas | |||
Sequence: MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQITLHILPPTQVAMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRMPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE |
Proteomic databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 15-138 | Acyltransferase | ||||
Sequence: RVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIE | ||||||
Region | 233-646 | AMP-binding | ||||
Sequence: SYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRMPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAI |
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)80,700
- Last updated1997-11-01 v2
- ChecksumF4F1021E57835EB2
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 15-16 | in Ref. 1; AAA17550 | ||||
Sequence: RV → AL | ||||||
Sequence conflict | 202 | in Ref. 1; AAA17550 | ||||
Sequence: P → S | ||||||
Sequence conflict | 281 | in Ref. 4; AAT42454 | ||||
Sequence: M → I |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L14681 EMBL· GenBank· DDBJ | AAA17550.1 EMBL· GenBank· DDBJ | Unassigned DNA | ||
U29581 EMBL· GenBank· DDBJ | AAB40483.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC75875.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE76905.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY625100 EMBL· GenBank· DDBJ | AAT42454.1 EMBL· GenBank· DDBJ | Genomic DNA |