ID I4VR10_9GAMM Unreviewed; 882 AA.
AC I4VR10;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000256|ARBA:ARBA00013432, ECO:0000256|HAMAP-Rule:MF_00393};
DE Short=GPAT {ECO:0000256|HAMAP-Rule:MF_00393};
DE EC=2.3.1.15 {ECO:0000256|ARBA:ARBA00013113, ECO:0000256|HAMAP-Rule:MF_00393};
GN Name=plsB {ECO:0000256|HAMAP-Rule:MF_00393};
GN ORFNames=UU7_16617 {ECO:0000313|EMBL:EIL89651.1};
OS Rhodanobacter spathiphylli B39.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1163407 {ECO:0000313|EMBL:EIL89651.1, ECO:0000313|Proteomes:UP000003226};
RN [1] {ECO:0000313|EMBL:EIL89651.1, ECO:0000313|Proteomes:UP000003226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B39 {ECO:0000313|EMBL:EIL89651.1,
RC ECO:0000313|Proteomes:UP000003226};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC Evidence={ECO:0000256|ARBA:ARBA00000510, ECO:0000256|HAMAP-
CC Rule:MF_00393};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC {ECO:0000256|ARBA:ARBA00004765, ECO:0000256|HAMAP-Rule:MF_00393}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00393};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00393};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_00393}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000256|HAMAP-Rule:MF_00393}.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC {ECO:0000256|ARBA:ARBA00007937, ECO:0000256|HAMAP-Rule:MF_00393}.
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:EIL89651.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJXT01000059; EIL89651.1; -; Genomic_DNA.
DR AlphaFoldDB; I4VR10; -.
DR STRING; 1163407.UU7_16617; -.
DR PATRIC; fig|1163407.3.peg.3339; -.
DR eggNOG; COG2937; Bacteria.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000003226; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR HAMAP; MF_00393; Glyc3P_acyltrans; 1.
DR InterPro; IPR022284; GPAT/DHAPAT.
DR InterPro; IPR045520; GPAT/DHAPAT_C.
DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR InterPro; IPR028354; GPAT_PlsB.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR NCBIfam; TIGR03703; plsB; 1.
DR PANTHER; PTHR12563:SF17; DIHYDROXYACETONE PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR12563; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF19277; GPAT_C; 1.
DR PIRSF; PIRSF500064; GPAT; 1.
DR PIRSF; PIRSF000437; GPAT_DHAPAT; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_00393};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00393}; Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00393};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00393};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00393};
KW Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00393};
KW Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_00393};
KW Reference proteome {ECO:0000313|Proteomes:UP000003226};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00393}.
FT DOMAIN 312..439
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 824..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 317..322
FT /note="HXXXXD motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00393"
FT COMPBIAS 851..882
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 882 AA; 98261 MW; 39E3146E16D28382 CRC64;
MPMITTADAP ARQPAPWWFN LAGQLLQPWV RIRRDPAEPA TLLQAGVPVC YVIERDGFSD
ALILQRACRE AGLPSPMQAL SGTRRRRSVF ALTRRDGWLF GRNRKRAASE PLRQLVHSLE
GQPELDVQIV PVSIYVGRAP SRDSGWFRVL FSENWVMVGR FGRLLALLLN GRDTVVHFSA
PVSLRQMLDE SGTIAPERFA RKVARVLRTH FHRIRAAVIG PDLSHKRTVV DSVLNAEPVR
AAIVAAAAKE KISHAKAWRK ANKLLLEIAA DYSHPVVRSA SFLLSNFWNK LYDGIAMHHF
DKARAAAPGH EVIYVPCHRS HADYLLMSYQ LHVSGVVVPH IAAGVNLNLP VIGPILRRGG
AFFLRRSFKG NALYSVVFNE YVAQLIDRGV PMEYFIEGGR SRTGRLLAPR AGMLVMTVRA
FLRAPRRPVL FQPVYIGYEK LMEGKSYAGE LSGQAKEKES LIGLLRGLKV LRQRYGHVAL
NFGEPIELTP LLDAASSDWR AAGADPDVKP EWLNSVTDRL AEQIQININR AADVNPINLL
ALALLATPKH AMAEADLLTQ LELGKAMLEE LPYSDRVTLT PMNPAAIIAY GEQMGWIQRV
QHPLGDVLTV GAEQAVLLSY FRNNVLHLNA TAAWVACCFL NNRRMSRASV LRLGQIIYPF
IQGELFLPWD ADGFVAQLEA TIDFFVRRGL LESTNDGRSL ERSPGQDDGA FQLKVIARSL
IQAFERYYIT IAALAKNGPH TMSGGELESA CTLTAQRLSL LNELSAPEFF DKALFRGFIQ
KLRERRIVWT DADGKLDYDS ALEGMVRDAR VILSREVRHS ILKITPGGER ETATEEPVDA
VPVQALPDDA SAADLHRRHV DAEQHEHERR SGDDRRGPTP DA
//
