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PLSB_VIBPA
ID   PLSB_VIBPA              Reviewed;         808 AA.
AC   Q87KN0;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2003, sequence version 1.
DT   25-MAY-2022, entry version 102.
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=VP2947;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; BA000031; BAC61210.1; -; Genomic_DNA.
DR   RefSeq; NP_799326.1; NC_004603.1.
DR   RefSeq; WP_005460370.1; NC_004603.1.
DR   AlphaFoldDB; Q87KN0; -.
DR   SMR; Q87KN0; -.
DR   STRING; 223926.28807973; -.
DR   EnsemblBacteria; BAC61210; BAC61210; BAC61210.
DR   GeneID; 1190533; -.
DR   KEGG; vpa:VP2947; -.
DR   PATRIC; fig|223926.6.peg.2836; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000002493; Chromosome 1.
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; Reference proteome; Transferase.
FT   CHAIN           1..808
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_0000195236"
FT   MOTIF           306..311
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   808 AA;  91143 MW;  96E9BAEA6DCE8B61 CRC64;
     MSSGQSFSRS LLKLPLSVMV KGTTIPSNPI DDLNIDLTKP IVYALPFRSN VDLLTLQKQA
     MSLGLPDPLS PLEINGKTLN RFVFIASRPT VMGNDNDIPT DSVSLFTELL ELHKLDSELD
     VQMIPATVLW GRKPGKEESH RPYLQPMNGP QKAKAVMAAG RDCLVRFSPV VSLRYMADSH
     GTDSAIAHKL ARVARIHFSR QKLAASGPNL PQRQVLFARL LKSPAIEQAI EDEAKSKDIS
     IEKARKEAHD IMDEIAADFS YGLVKNGDRI LSWLWTKLYQ GLHINNASTV RRLAQDGHEI
     VYVPCHRSHM DYLLLSYVLY HEGMVPPHIA AGINLNFFPA GPIFRRGGAF FIRRSFKGNK
     LYSTIFREYL AELFAKGYSV EYFSEGGRSR TGRLLQAKTG MLAMTIQAML RGLNRPVTLV
     PVYIGYEHVM EVGTYAKELR GKRKEKENAG LVLRTLRKLR NFGLGYVNFG EPIQLNQYLN
     EHAPEWTKDI DSMGGSKPQW MNPVVNELAN KMMTHINDAA AANALTLCAT ALLASRQRAL
     SRDSLINQIE CYLKLLKNNP YSSTSTIPTE SAEELVDHAI SLDKFVIETD SMGDIISLDR
     SQSILMTYYR NNIIHLFALP SLIAQMIIRQ RNLTVEKIQE NVAQIYPFLK KELFLSYQEE
     DLNDLVVKTL NEFAEQKMIC LDGNKLEINQ SNNQPLVLLG RTITETLQRY SIAMNLLVAY
     PELGKSDLEQ KSQDIAQRLG RLHGINAPEF FDKGVFTAMF NTLKQQEYLD SDGNCDKKKT
     QKFAKLLFTL LYPEVKLTIE ESIHQLQA
 
 
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