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PLSB_PSEU2
ID   PLSB_PSEU2              Reviewed;         833 AA.
AC   Q4ZWU3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
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}; OrderedLocusNames=Psyr_1328;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT   syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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: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; CP000075; AAY36379.1; -; Genomic_DNA.
DR   RefSeq; WP_011266965.1; NC_007005.1.
DR   RefSeq; YP_234417.1; NC_007005.1.
DR   AlphaFoldDB; Q4ZWU3; -.
DR   STRING; 205918.Psyr_1328; -.
DR   PRIDE; Q4ZWU3; -.
DR   EnsemblBacteria; AAY36379; AAY36379; Psyr_1328.
DR   KEGG; psb:Psyr_1328; -.
DR   PATRIC; fig|205918.7.peg.1361; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000000426; 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: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; IPR041728; GPAT/DHAPAT_LPLAT.
DR   InterPro; IPR045520; GPAT_C.
DR   InterPro; IPR028354; GPAT_PlsB.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR12563; PTHR12563; 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   TIGRFAMs; TIGR03703; plsB; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cell inner membrane; Cell membrane; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Transferase.
FT   CHAIN           1..833
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000049450"
FT   MOTIF           309..314
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   833 AA;  94717 MW;  73BF4192F906B936 CRC64;
     MTRSPFRRLV FGTLRRLLYL WVRSETINQS SFTLNLDRSR PVFYALQSPS ISDLAVIDTE
     CRKAGLPRPV LSVAVGNLIE PAAFFYLTPS PDWLGRQDKR GAPPTLERVV AAVSQNPGED
     AQIIPVSVFW GQSPDRESSA WKLLFADSWA VTGRLRRLVS ILILGRKTRV QFSAPIHMRE
     LVGENKGYEL TLRMTQRLLR VHFRNLKSAV IGPDVSHRRT VVKGLLDEPL VKQAIIEEAE
     REHITQEKAR ERALSYGNEI ASDYTYSVIR FMEVVLSWFW NKIYDGIKVS HIEGVQEVAP
     GHEVIYVPCH RSHIDYLLLS YLLFRNGLTP PHIAAGINLN MPVVGGLLRR GGAFFMRRTF
     KGNPLYTAVF TEYLHTLFIK GFPVEYFVEG GRSRTGRMLQ PKTGMLAITL RSFLRNSRMP
     IVFIPVYIGY ERVLEGRTYL GELRGATKKK ESIFDIFKVI GALKQRFGQV SVNFGAPIKL
     AEFLDGEQPD WREQQLDPQF RPEWLSETTH RLGERVAQHL NEAAAVNPMN LVAVALLSTQ
     RLALDDQAME RVLDLYLTLL RAVPYSPHTT LPEGDGRSLI EHVKGMDLLA EQKDALGKIL
     YLNEQNAVLM TYYRNNVLHI FALPSLLASF FQSSSRMTRE QILRYTRALY PFLQSELFIR
     WPLNELDDVV DQWLAAFVEQ GLLRFKKDAY VRPEPSSREF VLLTLLSRAI AQTLQRFYMA
     IALLLNSGQN TLSPEQLEDL CTVMAQRLSI LHGLNAPEFF DKSLFRHFIQ TLLDLGVLRK
     DSAGKLSYHP MLGELAEGAA KRVLPAEIRL SIRQVALHSN EEEQDVGTDQ GAA
 
 
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