(data stored in ACNUC7421 zone)

SWISSPROT: PLSB_SHESH

ID   PLSB_SHESH              Reviewed;         807 AA.
AC   A8FPP1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   30-AUG-2017, entry version 63.
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=Ssed_0201;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000821; ABV34814.1; -; Genomic_DNA.
DR   RefSeq; WP_012004340.1; NC_009831.1.
DR   ProteinModelPortal; A8FPP1; -.
DR   SMR; A8FPP1; -.
DR   STRING; 425104.Ssed_0201; -.
DR   EnsemblBacteria; ABV34814; ABV34814; Ssed_0201.
DR   KEGG; sse:Ssed_0201; -.
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; UP000002015; Chromosome.
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; A8FPP1.
DR   SWISS-2DPAGE; A8FPP1.
KW   Acyltransferase; Cell inner membrane; Cell membrane;
KW   Complete proteome; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Transferase.
FT   CHAIN         1    807       Glycerol-3-phosphate acyltransferase.
FT                                /FTId=PRO_1000080294.
FT   MOTIF       308    313       HXXXXD motif.
SQ   SEQUENCE   807 AA;  91667 MW;  6DB8A335BE6119B1 CRC64;
     MSKQDSLWFK SLRWLQNKLV HTIVVPHEPF KDLNLDPDKP LAYVMKTESV SDIAALSEIT
     ADLGLPSPYQ PLEVGGESAP RVVCLEGAKP LMGKRESNHF FLNSFMSLLK IHKERPELDI
     QLVPVSLYWG RTPGKEDDTM KAAVLERENP TWLRKCLMIL FLGRHNFVQF SSAVSLRYMA
     DEHGTDKRIA QKLARVARVH FSRQRKVMTG PVLPKRQALF HALINSETLK KAIQEEAASK
     KITEVEARAK AMEYLDEIAA DYSDSLVRIA ERFLTWLWNK LYKGINIKGA EEVRRLHHDG
     HEIIYVPCHR SHMDYLLLSY ILYYQGMVPP HIAAGINLNF WPAGPMFRRG GAFFIRRSFR
     GNKLYTTVFR EYLDQLFTKG YSVEYFTEGG RSRTGRLLAP KTGMLAMTLN SVLRGMKRPV
     TLVPVYLGYD HVMEVATYHK ELSGKKKKKE SVWQVFGALR KLGNFGQGYV NFGKPITLHS
     FLNEQKPDWK EEIAKEPEQR PKWLTPMVNT LANQVMTNIN DAAAVSSVTL TSLVLLASEQ
     NALERSQLEK QLDLYLKLLK DLPYTSYTSV VEGDGKSLVQ QGLELKKIKL DSDPLGDIIS
     IDESIAVAMT YYRNNIIHLM VIPSLVASCL TQHEHISRDE IIDIIKDFYP LLQAELFMGV
     EDTDKLVGQI LDLFIAQGLV TEDDGFSIIE TEVNQLLLLA GTVGETLQRY AIIFNLLAVC
     PKMERSDLER ESHKLAQRLG ALHGITAPEF YDKKLYGALS VKLKELGYLS DNGNKVDVQR
     IRERANGLLR SSVRQTIVDS VTAEHKD
//

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