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PLSB_SODGM
ID   PLSB_SODGM              Reviewed;         819 AA.
AC   Q2NR08;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=SG2142;
OS   Sodalis glossinidius (strain morsitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=343509;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=morsitans;
RX   PubMed=16365377; DOI=10.1101/gr.4106106;
RA   Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA   Aksoy S.;
RT   "Massive genome erosion and functional adaptations provide insights into
RT   the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL   Genome Res. 16:149-156(2006).
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; AP008232; BAE75417.1; -; Genomic_DNA.
DR   RefSeq; WP_011411954.1; NZ_LN854557.1.
DR   AlphaFoldDB; Q2NR08; -.
DR   SMR; Q2NR08; -.
DR   STRING; 343509.SG2142; -.
DR   EnsemblBacteria; BAE75417; BAE75417; SG2142.
DR   KEGG; sgl:SG2142; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   OrthoDB; 580383at2; -.
DR   BioCyc; SGLO343509:SGP1_RS19760-MON; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000001932; 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..819
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_1000049468"
FT   MOTIF           307..312
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   819 AA;  92471 MW;  D5F188D61C51763A CRC64;
     MSGWRRIYYT LLDLPLKLLV RSKVIPADPR AEAGLDPRQP MMYMLPYNSK ADLLTLRMQC
     LKQGLPDPLT PLDIDGVTLP RYVFIHDGPR VLTWYAEKSQ SVSLFHNYLD LHRSNPALDV
     QLVPVSVMFG RSPGRESQTS QPAPQLRLLN GIEKFFAVLW LGRDSFVRFS RPLSLRYMAT
     EHGTDKSIAQ KLARVARIHF ARQRLVAAGP RLPVRQDLFN KLLASKAIEK AVEDEARSKK
     ISVEKAQQNA IELMEEIAAD FSYEAIRLSD RVLSWTWNRL YQGLHVRNAE RVRQLAEEGH
     EIVYVPCHRS HMDYLLLSYV LYHQGLVPPH IAAGINLNFW PAGPIFRRLG AFFIRRTFKG
     NKLYSTIFRE YLGELFTRGY SVEYFVEGGR SRTGRLLEPK TGTLTMTIQA MLRGGNRPIT
     LVPIYVGYEH VMEVATYAKE LRGAAKEKEG LWQMMRGLRK LRNLGQGYVN FGDPLPLATW
     LSQQVPQWRD SIDPIEAQRP SWLAPAVDEI AATLMVRINN AAAANAINLC SSVLLASRQR
     SLTRPHLLAQ LACYFELLRN VPYAPDITVP DLTPEALLAH ALAMNKFTVE HDTIGDIICL
     SRDQAVLMTY YRNNIQHLLI LPSLVASIIC GHPGIERAQL QQRITLLYPL LKAELFMRYS
     KQELSPVIDS LIAELARQGL VDAQETRLYP AQTRLHVLQL LAASVRETLQ RYAITFSLLR
     ANPQLNRGTL EKESRIMAQR LSVLHGINAP EFFDKAVFST LVATLRAEEY ISDTGDAIDE
     KVSEMCDILS ELITPDVLGT IESASLLAHG PASAALPAD
 
 
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