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Database: UniProt
Entry: A4XWR9
LinkDB: A4XWR9
Original site: A4XWR9 
ID   ISPD_PSEMY              Reviewed;         235 AA.
AC   A4XWR9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   29-OCT-2014, entry version 55.
DE   RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_00108};
DE            EC=2.7.7.60 {ECO:0000255|HAMAP-Rule:MF_00108};
DE   AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase {ECO:0000255|HAMAP-Rule:MF_00108};
DE   AltName: Full=MEP cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_00108};
DE            Short=MCT {ECO:0000255|HAMAP-Rule:MF_00108};
GN   Name=ispD {ECO:0000255|HAMAP-Rule:MF_00108};
GN   OrderedLocusNames=Pmen_3031;
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ymp;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C.,
RA   Bruce D., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Hersman L., Dubois J., Maurice P.,
RA   Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-
CC       methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-
CC       phosphate (MEP). {ECO:0000255|HAMAP-Rule:MF_00108}.
CC   -!- CATALYTIC ACTIVITY: CTP + 2-C-methyl-D-erythritol 4-phosphate =
CC       diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol.
CC       {ECO:0000255|HAMAP-Rule:MF_00108}.
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
CC       biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
CC       deoxy-D-xylulose 5-phosphate: step 2/6. {ECO:0000255|HAMAP-
CC       Rule:MF_00108}.
CC   -!- SIMILARITY: Belongs to the IspD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00108}.
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DR   EMBL; CP000680; ABP85785.1; -; Genomic_DNA.
DR   RefSeq; YP_001188517.1; NC_009439.1.
DR   ProteinModelPortal; A4XWR9; -.
DR   STRING; 399739.Pmen_3031; -.
DR   EnsemblBacteria; ABP85785; ABP85785; Pmen_3031.
DR   GeneID; 5107511; -.
DR   KEGG; pmy:Pmen_3031; -.
DR   PATRIC; 19912674; VBIPseMen131592_3077.
DR   eggNOG; COG1211; -.
DR   HOGENOM; HOG000218564; -.
DR   KO; K00991; -.
DR   OMA; KADRPKQ; -.
DR   OrthoDB; EOG6J48RZ; -.
DR   BioCyc; PMEN399739:GHR6-3090-MONOMER; -.
DR   UniPathway; UPA00056; UER00093.
DR   GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IEA:UniProtKB-HAMAP.
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-HAMAP.
DR   Gene3D; 3.90.550.10; -; 1.
DR   HAMAP; MF_00108; IspD; 1.
DR   InterPro; IPR001228; IspD.
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   Complete proteome; Isoprene biosynthesis; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN         1    235       2-C-methyl-D-erythritol 4-phosphate
FT                                cytidylyltransferase.
FT                                /FTId=PRO_1000202896.
FT   SITE         17     17       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00108}.
FT   SITE         24     24       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00108}.
FT   SITE        158    158       Positions MEP for the nucleophilic
FT                                attack. {ECO:0000255|HAMAP-
FT                                Rule:MF_00108}.
FT   SITE        214    214       Positions MEP for the nucleophilic
FT                                attack. {ECO:0000255|HAMAP-
FT                                Rule:MF_00108}.
SQ   SEQUENCE   235 AA;  25629 MW;  A07F6FADA7F51FB9 CRC64;
     MSTKFWLVVP AAGVGARMAA DRPKQYLQVG GRCIIEHTLD CFLDHPDLLG AVVCLAVDDP
     YWPQLAVASD PRVRRAPGGR ERADSVLAGL DALQAAGAGE QDWVLVHDAA RPNLAREDLQ
     RLLAVLADDP VGGLLAVPVR DTLKRADADG RVAQTVDRSQ IWQAYTPQMF RLGALSQALR
     GALAAGVPIT DEASALEWCG QSSRLVEGRA DNLKITRPED LAWLRQAWVE RDRQR
//
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