AC   MF_01162;
DC   Protein; auto
TR   HAMAP; MF_01162; -; 1; level=0
XX
Names: Aas
XX
ID   AAS
DE   RecName: Full=Bifunctional protein Aas;
DE   Includes:
DE     RecName: Full=2-acylglycerophosphoethanolamine acyltransferase;
DE              EC=2.3.1.40;
DE     AltName: Full=2-acyl-GPE acyltransferase;
DE     AltName: Full=Acyl-[acyl-carrier-protein]--phospholipid O-acyltransferase;
DE   Includes:
DE     RecName: Full=Acyl-[acyl-carrier-protein] synthetase;
DE              EC=6.2.1.20;
DE     AltName: Full=Acyl-ACP synthetase;
DE     AltName: Full=Long-chain-fatty-acid--[acyl-carrier-protein] ligase;
GN   Name=aas;
XX
CC   -!- FUNCTION: Plays a role in lysophospholipid acylation. Transfers fatty
CC       acids to the 1-position via an enzyme-bound acyl-ACP intermediate in
CC       the presence of ATP and magnesium. Its physiological function is to
CC       regenerate phosphatidylethanolamine from 2-acyl-glycero-3-
CC       phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or
CC       degradation by phospholipase A1.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-acyl-sn-glycero-3-phosphoethanolamine + a fatty acyl-[ACP]
CC         = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + holo-[ACP];
CC         Xref=Rhea:RHEA:10304, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:14125,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:64612, ChEBI:CHEBI:65213,
CC         ChEBI:CHEBI:138651; EC=2.3.1.40;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain fatty acid + ATP + holo-[ACP] = a long-chain
CC         fatty acyl-[ACP] + AMP + diphosphate; Xref=Rhea:RHEA:45588,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:12682, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57560, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:133243, ChEBI:CHEBI:456215; EC=6.2.1.20;
case not defined <Property:Membrane> or <Property:Membrane=1>
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
else case <Property:Membrane=2>
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
end case
CC   -!- SIMILARITY: In the N-terminal section; belongs to the 2-acyl-GPE
CC       acetyltransferase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the ATP-dependent
CC       AMP-binding enzyme family.
XX
DR   Pfam; PF01553; Acyltransferase; 1; trigger=no
DR   Pfam; PF00501; AMP-binding; 1; trigger=no
DR   PRINTS; PR00154; AMPBINDING; 1; trigger=no
DR   PROSITE; PS00455; AMP_BINDING; 1; trigger=no
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KW   Acyltransferase
KW   ATP-binding
KW   Nucleotide-binding
case defined <Property:Membrane> and <Property:Membrane=2>
KW   Cell inner membrane
end case
KW   Cell membrane
KW   Ligase
KW   Membrane
KW   Multifunctional enzyme
KW   Transferase
KW   Transmembrane
KW   Transmembrane helix
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GO   GO:0008779; F:acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase activity
GO   GO:0008922; F:long-chain fatty acid [acyl-carrier-protein] ligase activity
GO   GO:0005886; C:plasma membrane
XX
FT   From: AAS_ECOLI (P31119)
FT   TRANSMEM        258..277
FT                   /note="Helical"
FT   TRANSMEM        409..433
FT                   /note="Helical"
FT   REGION          15..138
FT                   /note="Acyltransferase"
FT   REGION          233..646
FT                   /note="AMP-binding"
FT   ACT_SITE        36
FT   Condition: H
XX
Size: 718-738;
Related: None;
Template: P31119;
Scope:
 Bacteria; Enterobacterales
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.33 2019/11/19
//