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PLSB_HAEIN
ID   PLSB_HAEIN              Reviewed;         810 AA.
AC   P44857;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase;
DE            Short=GPAT;
DE            EC=2.3.1.15;
GN   Name=plsB; OrderedLocusNames=HI_0748;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000305}.
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DR   EMBL; L42023; AAC22406.1; -; Genomic_DNA.
DR   PIR; D64090; D64090.
DR   RefSeq; NP_438907.1; NC_000907.1.
DR   RefSeq; WP_005693149.1; NC_000907.1.
DR   AlphaFoldDB; P44857; -.
DR   SMR; P44857; -.
DR   STRING; 71421.HI_0748; -.
DR   DNASU; 949773; -.
DR   EnsemblBacteria; AAC22406; AAC22406; HI_0748.
DR   KEGG; hin:HI_0748; -.
DR   PATRIC; fig|71421.8.peg.785; -.
DR   eggNOG; COG2937; Bacteria.
DR   HOGENOM; CLU_015407_0_0_6; -.
DR   OMA; EVIYVPC; -.
DR   PhylomeDB; P44857; -.
DR   BioCyc; HINF71421:G1GJ1-786-MON; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IBA:GO_Central.
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   GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; IBA:GO_Central.
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..810
FT                   /note="Glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_0000195222"
FT   MOTIF           306..311
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   810 AA;  92775 MW;  DB8564BC3E2C370D CRC64;
     MANFINMYRQ LLSLPLSALV KNNPIPANPI EELSLNIHQP IVYVLPYTSQ TDFVIFRRNC
     LALGLPDPAE KNEINGVKLP RYVYLDEGRR IFKSKGAKDE TTTIFNKYLE LHRTSESLDV
     QLIPVSVLWG RSPGQEDKSD LPNLRLLNGI QKTFAAIWFG RDTFVRFSQA VSLRYMVVEH
     GSDEKIAQKL ARVAKMHFAK QRISATGPRL PNRQAMFNKL LQSEAIRRAI EDEAKSKNIS
     IEKAQKEAYK ILDEIAADVS HSSLRAVDRF LRWLWNKLYS GINVQNSNRV RKLALEGHEI
     VYVPCHRSHI DYLLLSYVLY HQGLVPPHIA AGINLNFWPI GRMFRSWGAF FIRRTFKGNR
     LYSAIFREYL SELFHRGYSV EYFIEGGRSR TGRLLAPKTG MMSMTLQALQ HSQTRPISIV
     PVYVGYEHVL EVDTYAKELR GAAKEKENAG LVLRVIKKLR NLGQGFVNFG EPITLSNYLS
     QHFPDWKEQN HEEKPQWFTP AVNNISKQVM ININKAAAVN SMNLVGTALL SSRQRALSRE
     QLLEQLSSYQ QLLQNVPYST DVVLPNVTPQ AMLEHVLALD RIGVLIEKDN FGEIVRLERS
     SAVLMTYYRN NIQHLFVLPS LVASIILHYE AIQKDLLLDA IRKIYPFLQG ELFLHFNEDE
     LNVQIHQIIN EFARQSVINS NDNFLSINKS KVRILQLWSA GMLEILQRYY ITVTILQKQP
     AISRAELEKE SQLVAQRLSV LHGINAPEFF DKAVFSSFIA NLKEQRYFDE SGYTVLDKIE
     ELASTLSHLI STEICLTVKG TIEKSEDLSS
 
 
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