(data stored in ACNUC7421 zone)

SWISSPROT: PLSB_EDWI9

ID   PLSB_EDWI9              Reviewed;         818 AA.
AC   C5B706;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   30-AUG-2017, entry version 47.
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=NT01EI_0225;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) 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; CP001600; ACR67468.1; -; Genomic_DNA.
DR   RefSeq; WP_015869677.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0225; -.
DR   PRIDE; C5B706; -.
DR   EnsemblBacteria; ACR67468; ACR67468; NT01EI_0225.
DR   GeneID; 7960249; -.
DR   KEGG; eic:NT01EI_0225; -.
DR   PATRIC; fig|634503.3.peg.201; -.
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; UP000001485; 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; C5B706.
DR   SWISS-2DPAGE; C5B706.
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    818       Glycerol-3-phosphate acyltransferase.
FT                                /FTId=PRO_1000205849.
FT   MOTIF       305    310       HXXXXD motif.
SQ   SEQUENCE   818 AA;  92827 MW;  C22D7ADC3D55C290 CRC64;
     MSGWRKIYYK LLNLILKLLV KSKVIPTDPV AELRLDTTRP VFYVLPYNSK VDLLTLRDRC
     LALDLPDPLD DNEIDGVILP RYVFIDDGPR VFRYYAPKQA SVKLFLDYLD LHRGNPSLDI
     QMIPVSVMFG RAPGREDHKG APQLRLLNGI QKFFAVLWLG RDSFVRFSNT VSLRYMADEH
     GTDKTIAQKL ARVARMHFSR LRLAAVGPRL PDRQALFNKL LGSKAIEKAV EDEARSKKIS
     REKAQQNAVA LMEEIAADFT YEAVRLSDRV LSWTWNRLYQ GINVHNAERV RQLAQDGHEI
     VYVPCHRSHM DYLLLSYVLY HQGLVPPHIA AGINLNFWPA GPIFRRLGAF FIRRTFKGNK
     LYSTVFREYL GELFSRGYSV EYFMEGGRSR TGRLLEPKTG TLAMTLQAML RGGKRPITLV
     PVYIGYEHVM EVATYAKELR GATKEKESLP QMVRGLRKLR NLGQGYVNFG EPISLNVWLN
     QHVPEWREAI DPIEAQRPHW LPASVNSIAG EVMVNINKAA AANAMNLCAT ALLASRQRAL
     TREQLLEQLE CYLQLLQNVP YAPDATLPQR TPQELLDHAL QMNKFEVEKD NIGDLIILPR
     EQAVLMTYYR NNIQHMLVLP ALVASMVIHH RQISRDELLR QAAVIYPMLK QELFMHYVPE
     TLPQVLSPII DELCRQQLIS LQDDTLIINP PRIRSLQLLA AGVRETLQRY AITFSLLSAN
     PSISRGALEK ESRILAQRLS LLHGINAPEF FDKAVFATLV ATLRAEGYIN DVGDAVREQT
     LEIYNLLADL LTPEIRLTIE SVSIAALEDT GGADGGTA
//

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