ID A0A0J5M1U4_PLUGE Unreviewed; 719 AA.
AC A0A0J5M1U4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Bifunctional protein Aas {ECO:0000256|HAMAP-Rule:MF_01162};
DE Includes:
DE RecName: Full=2-acylglycerophosphoethanolamine acyltransferase {ECO:0000256|HAMAP-Rule:MF_01162};
DE EC=2.3.1.40 {ECO:0000256|HAMAP-Rule:MF_01162};
DE AltName: Full=2-acyl-GPE acyltransferase {ECO:0000256|HAMAP-Rule:MF_01162};
DE AltName: Full=Acyl-[acyl-carrier-protein]--phospholipid O-acyltransferase {ECO:0000256|HAMAP-Rule:MF_01162};
DE Includes:
DE RecName: Full=Acyl-[acyl-carrier-protein] synthetase {ECO:0000256|HAMAP-Rule:MF_01162};
DE EC=6.2.1.20 {ECO:0000256|HAMAP-Rule:MF_01162};
DE AltName: Full=Acyl-ACP synthetase {ECO:0000256|HAMAP-Rule:MF_01162};
DE AltName: Full=Long-chain-fatty-acid--[acyl-carrier-protein] ligase {ECO:0000256|HAMAP-Rule:MF_01162};
GN Name=aas {ECO:0000256|HAMAP-Rule:MF_01162};
GN ORFNames=ABW06_04640 {ECO:0000313|EMBL:KMK15270.1};
OS Pluralibacter gergoviae (Enterobacter gergoviae).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Pluralibacter.
OX NCBI_TaxID=61647 {ECO:0000313|EMBL:KMK15270.1, ECO:0000313|Proteomes:UP000036196};
RN [1] {ECO:0000313|EMBL:KMK15270.1, ECO:0000313|Proteomes:UP000036196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS81F13 {ECO:0000313|EMBL:KMK15270.1,
RC ECO:0000313|Proteomes:UP000036196};
RA Greninger A.L., Miller S.;
RT "Genome sequences of Pluralibacter gergoviae.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|HAMAP-Rule:MF_01162}.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01162};
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;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01162};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01162};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01162}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the ATP-dependent
CC AMP-binding enzyme family. {ECO:0000256|HAMAP-Rule:MF_01162}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the 2-acyl-GPE
CC acetyltransferase family. {ECO:0000256|HAMAP-Rule:MF_01162}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMK15270.1}.
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DR EMBL; LDZF01000004; KMK15270.1; -; Genomic_DNA.
DR RefSeq; WP_048278314.1; NZ_VWRP01000028.1.
DR AlphaFoldDB; A0A0J5M1U4; -.
DR STRING; 61647.LG71_09105; -.
DR PATRIC; fig|61647.15.peg.3770; -.
DR eggNOG; COG0204; Bacteria.
DR eggNOG; COG0318; Bacteria.
DR Proteomes; UP000036196; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008779; F:acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008922; F:long-chain fatty acid [acyl-carrier-protein] ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR HAMAP; MF_01162; Aas; 1.
DR InterPro; IPR023775; Aas.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR43767; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR PANTHER; PTHR43767:SF1; NONRIBOSOMAL PEPTIDE SYNTHASE PES1 (EUROFUNG)-RELATED; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01162};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01162}; Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01162};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01162};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01162, ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_01162};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01162}; Reference proteome {ECO:0000313|Proteomes:UP000036196};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01162};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01162};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01162}.
FT TRANSMEM 258..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 415..438
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..140
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 15..138
FT /note="Acyltransferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01162"
FT REGION 233..646
FT /note="AMP-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01162"
FT ACT_SITE 36
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01162"
SQ SEQUENCE 719 AA; 79837 MW; DFD4E4279539B4EE CRC64;
MLIGFFRLLF KAMFRVRLTG DTDALRLPKV LITPNHVSFL DGMLLALFLP GRPVFAVYTS
ISEKWFMRAI KPLIDFVPLD PTKPMSIKHL VRLVDQGRPV VIFPEGRITV SGSLMKIYDG
AAFVAAKSQA TVVPLRIEGA ELTFASRLKG LVKRRLFPRI SLHLLPPTQL PMPDAPRARD
RRRIAGEMLH QIMMEARMAV RPRETLYEAL LSAQYRFGDR KPCVEDINFQ PDSYRKLLTK
TLFVARILEK YSQPGERIGL MLPNAGISAA VIFGAVARRR IPAMMNYTAG VKGLSSAITA
AEIKTIFTSR TFLDKGKLWH LPEQLTQVRW VFLEDLKGDV TAADKLWIFG HLLMPHLAQV
PQRPEDDAII LFTSGSEGHP KGVVHSHKSI LANVEQIKTI ADFTAADRFM SALPLFHSFG
LTVGLFTPLF TGAQVFLYPS PLHYRIVPEL VYDRNCTVLF GTSTFLGNYA RFANPYDFFK
VRYVVAGAEK LQESTKQLWQ DKFGLRILEG YGVTECAPVV SINVPMAAKP GTVGRILPGM
DARLMAVPGI EQGGRLQLKG PNIMNGYLRV EKPGVLEAPA AENPQGLLEA GWYDTGDIVA
FDEQGFVQIQ GRAKRFAKIA GEMVSLEIVE QLALAVSPDK MHATAIKQDA SKGEALVLFT
TDAELTREQL LQKARAGGVP ELAVPRDIRF LKQMPLLGSG KPDFVTLKGM VDEGEKSDE
//
