位置:首页 > 蛋白库 > ISPD_HAEIN
ISPD_HAEIN
ID   ISPD_HAEIN              Reviewed;         225 AA.
AC   O05029;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase;
DE            EC=2.7.7.60;
DE   AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase;
DE   AltName: Full=MEP cytidylyltransferase;
DE            Short=MCT;
GN   Name=ispD; OrderedLocusNames=HI_0672;
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   -!- FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-
CC       erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-
CC         methyl-D-erythritol + diphosphate; Xref=Rhea:RHEA:13429,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC         ChEBI:CHEBI:57823, ChEBI:CHEBI:58262; EC=2.7.7.60;
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC       phosphate: step 2/6.
CC   -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L42023; AAC22332.1; -; Genomic_DNA.
DR   PIR; G64156; G64156.
DR   RefSeq; NP_438832.1; NC_000907.1.
DR   RefSeq; WP_005655267.1; NC_000907.1.
DR   AlphaFoldDB; O05029; -.
DR   SMR; O05029; -.
DR   STRING; 71421.HI_0672; -.
DR   EnsemblBacteria; AAC22332; AAC22332; HI_0672.
DR   KEGG; hin:HI_0672; -.
DR   PATRIC; fig|71421.8.peg.702; -.
DR   eggNOG; COG1211; Bacteria.
DR   HOGENOM; CLU_061281_3_1_6; -.
DR   OMA; ERQHSVY; -.
DR   PhylomeDB; O05029; -.
DR   BioCyc; HINF71421:G1GJ1-707-MON; -.
DR   UniPathway; UPA00056; UER00093.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IBA:GO_Central.
DR   GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02516; CDP-ME_synthetase; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   HAMAP; MF_00108; IspD; 1.
DR   InterPro; IPR001228; IspD.
DR   InterPro; IPR034683; IspD/TarI.
DR   InterPro; IPR018294; ISPD_synthase_CS.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF01128; IspD; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR00453; ispD; 1.
DR   PROSITE; PS01295; ISPD; 1.
PE   3: Inferred from homology;
KW   Isoprene biosynthesis; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..225
FT                   /note="2-C-methyl-D-erythritol 4-phosphate
FT                   cytidylyltransferase"
FT                   /id="PRO_0000075579"
FT   SITE            17
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   SITE            24
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   SITE            150
FT                   /note="Positions MEP for the nucleophilic attack"
FT                   /evidence="ECO:0000250"
FT   SITE            206
FT                   /note="Positions MEP for the nucleophilic attack"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   225 AA;  24548 MW;  2155A297B44CD8C9 CRC64;
     MARSIIAVLP AAGVGSRMQA DKPKQYLTLL GKTLLEHTLD VMLSYPAVSK IILAVSKDDP
     YISTLSLDPK IQLVEGGTTR AESVLNGLNA IAEKNAWVLV HDAARPCLQH ADIDKLLAIE
     DKQGAILAIP VTDTIKRADN QQCIVKTEDR SQLWQAMTPQ FFPVDILRDA LSTGIQQGAN
     ITDEASAIEL AGFRPHLVAG RSDNLKVTRP EDLALAEFYL TRNKL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024