ID L0MIP9_9GAMM Unreviewed; 718 AA.
AC L0MIP9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 71.
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=D781_3573 {ECO:0000313|EMBL:AGB83778.1};
OS Serratia sp. FGI94.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=671990 {ECO:0000313|EMBL:AGB83778.1, ECO:0000313|Proteomes:UP000011001};
RN [1] {ECO:0000313|EMBL:AGB83778.1, ECO:0000313|Proteomes:UP000011001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGI94 {ECO:0000313|EMBL:AGB83778.1,
RC ECO:0000313|Proteomes:UP000011001};
RX PubMed=23516234;
RA Aylward F.O., Tremmel D.M., Starrett G.J., Bruce D.C., Chain P., Chen A.,
RA Davenport K.W., Detter C., Han C.S., Han J., Huntemann M., Ivanova N.N.,
RA Kyrpides N.C., Markowitz V., Mavrommatis K., Nolan M., Pagani I., Pati A.,
RA Pitluck S., Teshima H., Deshpande S., Goodwin L., Woyke T., Currie C.R.;
RT "Complete Genome of Serratia sp. Strain FGI 94, a Strain Associated with
RT Leaf-Cutter Ant Fungus Gardens.";
RL Genome Announc. 1:E0023912-E0023912(2013).
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}.
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DR EMBL; CP003942; AGB83778.1; -; Genomic_DNA.
DR RefSeq; WP_015673603.1; NC_020064.1.
DR AlphaFoldDB; L0MIP9; -.
DR KEGG; smaf:D781_3573; -.
DR PATRIC; fig|1249634.3.peg.3424; -.
DR eggNOG; COG0204; Bacteria.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_8_6; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000011001; Chromosome.
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; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR43201:SF5; MEDIUM-CHAIN ACYL-COA LIGASE ACSF2, MITOCHONDRIAL; 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|HAMAP-Rule:MF_01162, ECO:0000313|EMBL:AGB83778.1};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01162};
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}; 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 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 718 AA; 79822 MW; 3842B9F2C05C68D1 CRC64;
MFMSAMRALF RLLFRVRVEG DARHLNQQKL LITPNHVSFL DGVLLALFLP IKPVFAVYSS
VSDSWFMRWL KPYIDFVFLD PTKPMAVKHL VREVQQGRPI VVFPEGRITV TGSLMKVYDG
AAFIAAKSGA TVVPIRIDGP EFSPFGRMKG IFKLRAFPQI TLHILPPTLL PMPEAPRARE
RRELAGDHLY QIMLQARMAT RQPQTLFGAL LAAQKRYGAG KPCIEDIAFK EDNYRTLIKK
SLGVSRILQR FTAEGEHVGM LLPNATITAA AIFGASLRRR IPAMLNYTAG SNGLKSAMTA
ATIKTIVTSR QFLEKGKLTH LPEQVPEANW VYLEDLKDTV TLEDKLWILR HLLQPQRAML
PQQADDAALV LFTSGSEGHP KGVVHSHASL LANVEQIRTI ADFTPRDRFM SSLPLFHSFG
LTVGLLTPLM TGSRVFLYPS PLHYRVVPEL VYDLNCTVLF GTATFLNNYA RFAHPYDFAR
VRYVVAGAEK LAESTKQIYQ DKYGIRILEG YGVTECAPVV SINVPLATKV GTVGRIMPQM
EARLMPVAGI EEGGRLQLRG PNIMKGYLRV ERPGELEPPA AEDENGILQP GWYDTGDIVT
LDAQGYCTIR GRVKRFAKLA GEMISLEIVE QLALRASPDG HHAATVKSDS SKGEALVLYT
TDSELTRDAL LRVAREQGTP ELAVPRDIRW LKALPVLGSG KPDYVTLRKM AEQPESAS
//
