ID   PLSB_COLP3              Reviewed;         811 AA.
AC   Q48AL2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   02-SEP-2026, entry version 105.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_00393};
DE            Short=GPAT {ECO:0000255|HAMAP-Rule:MF_00393};
DE            EC=2.3.1.15 {ECO:0000255|HAMAP-Rule:MF_00393};
GN   Name=plsB {ECO:0000255|HAMAP-Rule:MF_00393};
GN   OrderedLocusNames=CPS_0133;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Alteromonadales; Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=34H / ATCC BAA-681;
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=sn-glycerol 3-phosphate + an acyl-CoA = 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:0000255|HAMAP-Rule:MF_00393};
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC       {ECO:0000255|HAMAP-Rule:MF_00393}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00393}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00393}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00393}.
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:0000255|HAMAP-Rule:MF_00393}.
CC   -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000255|HAMAP-
CC       Rule:MF_00393}.
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DR   EMBL; CP000083; AAZ27641.1; -; Genomic_DNA.
DR   RefSeq; WP_011041008.1; NC_003910.7.
DR   AlphaFoldDB; Q48AL2; -.
DR   SMR; Q48AL2; -.
DR   STRING; 167879.CPS_0133; -.
DR   KEGG; cps:CPS_0133; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000000547; Chromosome.
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:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:TreeGrafter.
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   InterPro; IPR060304; PlsB_N.
DR   NCBIfam; TIGR03703; plsB; 1.
DR   NCBIfam; NF003441; PRK04974.1; 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   Pfam; PF27464; PlsB_N; 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; Cell inner membrane; Cell membrane; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Reference proteome; Transferase.
FT   CHAIN           1..811
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000049429"
FT   MOTIF           309..314
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   811 AA;  91530 MW;  8D4D8AA84F1B673B CRC64;
     MLALRSFFYL LLKFPLKLLV RCKIITDSQN ITDQPNQPIF YIVRHQSASD LLALQSACKK
     QNLPDPLGKV TINGESFNRT LCLAKSTPLC SWRKSSKTTA TAQGLALLNQ HVIDENIDAK
     LIPANLIWGR TPTKERKNLN IGTLLADQES PNWLRKFFIV LFLGRDTLVR FSEAFSLRNI
     SDNHGSDEAA AHKFLRVARF HFHRQTIAAK GPRLMHRKQM FTALFANPSV KRIISDEAKN
     KKVSEAEIKK KALVMMNEIA GDYSVSWLRF GEIILHWLWK RLYSAIKVSN AKVLRKLAQD
     GHEIIYVPCH RSHMDYLLLS YVILQEGLVM PRIAAGINLN FWPAGTIFRK GGAFFIRRSF
     GGNRLYSTIF REYLGLLFER GYGVKYYTEG GRSRTGRVLA PKTGMLAMTI QSLLRGIDRP
     LTLVPVYLGY EHVMEVGTYH KELSGSEKKG ESMFGVLKAI KSLRNYGNGY VNFGEPMNIN
     EFLNKQVPDW KDSIDPIDPQ KPSWLTPTVN VLADQVMENI NKSAALNGVA LIALILHASK
     NKALSKLELE TQLDFFLNIQ RQAPFSEQLT IPEETGAELL THVISLNKVT ITEDSFGSLV
     SLSETANTEM RYYRNNILHT YVVPALVCRL LDKHSKINQD ELVIKVQNVT ALLKEDLYLY
     QDSTHVEQQT LRVLTVLKEM EIAKQTKAGF WSLSDDVGLL SQVHAMAECI DESLQRLAII
     TSLTSRLAPL SKRDLETKVV AIAKRLSVLN NINAPEFIDK RAQSTLIATI REQGYIDLDD
     DGLLIASSTM AEIKATVINL VDIEVLQSIA R
//