(data stored in ACNUC7421 zone)

SWISSPROT: PLSB_PSEHT

ID   PLSB_PSEHT              Reviewed;         812 AA.
AC   Q3IF27;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   30-AUG-2017, entry version 75.
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=PSHAa0142;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-
CC       acyl-sn-glycerol 3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00393}.
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis;
CC       CDP-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-
CC       Rule:MF_00393}.
CC   -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity
CC       and may constitute the binding site for the phosphate moiety of
CC       the glycerol-3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00393}.
CC   -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000255|HAMAP-
CC       Rule:MF_00393}.
DR   EMBL; CR954246; CAI85246.1; -; Genomic_DNA.
DR   RefSeq; WP_011326864.1; NC_007481.1.
DR   STRING; 326442.PSHAa0142; -.
DR   PRIDE; Q3IF27; -.
DR   EnsemblBacteria; CAI85246; CAI85246; PSHAa0142.
DR   KEGG; pha:PSHAa0142; -.
DR   PATRIC; fig|326442.8.peg.136; -.
DR   eggNOG; ENOG4105E55; Bacteria.
DR   eggNOG; COG2937; LUCA.
DR   HOGENOM; HOG000218231; -.
DR   KO; K00631; -.
DR   OMA; EVIYVPC; -.
DR   OrthoDB; POG091H06BX; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
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   HAMAP; MF_00393; Glyc3P_acyltrans; 1.
DR   InterPro; IPR022284; GPAT/DHAPAT.
DR   InterPro; IPR028354; GPAT_PlsB.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR12563; PTHR12563; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   PIRSF; PIRSF500064; GPAT; 1.
DR   PIRSF; PIRSF000437; GPAT_DHAPAT; 1.
DR   SMART; SM00563; PlsC; 1.
DR   TIGRFAMs; TIGR03703; plsB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IF27.
DR   SWISS-2DPAGE; Q3IF27.
KW   Acyltransferase; Cell inner membrane; Cell membrane;
KW   Complete proteome; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Phospholipid biosynthesis; Phospholipid metabolism;
KW   Reference proteome; Transferase.
FT   CHAIN         1    812       Glycerol-3-phosphate acyltransferase.
FT                                /FTId=PRO_1000049446.
FT   MOTIF       308    313       HXXXXD motif.
SQ   SEQUENCE   812 AA;  92076 MW;  1751179DED26D381 CRC64;
     MRIVNYCLNV LSAGVSRLLV RSKVLPEKPT EQYELNSKNP TFYIVRLNSR FDLAALARVC
     KRHGLPDPRE QQVLGTQRLD RFIGIENPPP LIGDIAKPTN ALAQGKQIID HLLSSGQKDV
     QVIPVTILWG RAPGKEKPGL STLITHSLTP SWFRKLFVVL FSGRDNFIRF SQPLDLSLLV
     DEKADVNELP QKLLRVARVH FRRQKLAATG PKMPSREQLF NSLLASPTIK KAIQDEAKAK
     NISQAQARQN AVKLLNEIAA NYSEAMIRVA ERFLTWLWNK LYNGIDIKYT EQIHELTNKG
     HEIIYMPCHR SHMDYLLLTY AIYHQGLVPP HIAAGINLNF FPAGGIFRRS GAFFIRRSFA
     GNKLYSAVFK EYLSQLFIKG YSVKFYTEGG RSRTGRLLPP KTGMLAMTMQ AMLRGIDRPI
     SIVPVYIGYE HVMEINTYLK ELAGNDKKGE SIFGIFKAIK NLKNYGRGYL NFGDPISINQ
     YLNDNQPNWR DDIHPTDVQK PQWLGPQVAN LADQVMVKIN NAAALNAVNL LAMILLVNDK
     HALSKPKLLA QLDFYLRLQR DASYSNKVTA PEETPEQLLT HALKLNKFDV ISDEFGEIIA
     INDKEKTLFN YYRNNILHLF AVPSLIALHL FREKTTTVSK CQQLVAAFYP LFAKEWYLRE
     LDEDYITRIL ANFVDQNLIE LDGDNIHITN TNDCLAKLDM LGKALNFTLQ RYAIVIGFIQ
     TSNGIEKAEL ERESQVLAQR LGTLHGIKTP EFFDKKVLVS FIDNLRAQSL ITDGDAGLIG
     SVQLCETYMH LKALLPARVW QSISDIVQGQ CK
//

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