GenomeNet

Database: UniProt/SWISS-PROT
Entry: ISPE_PELCD
LinkDB: ISPE_PELCD
Original site: ISPE_PELCD 
ID   ISPE_PELCD              Reviewed;         280 AA.
AC   Q3A311;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   01-OCT-2014, entry version 57.
DE   RecName: Full=4-diphosphocytidyl-2-C-methyl-D-erythritol kinase {ECO:0000255|HAMAP-Rule:MF_00061};
DE            Short=CMK {ECO:0000255|HAMAP-Rule:MF_00061};
DE            EC=2.7.1.148 {ECO:0000255|HAMAP-Rule:MF_00061};
DE   AltName: Full=4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase {ECO:0000255|HAMAP-Rule:MF_00061};
GN   Name=ispE {ECO:0000255|HAMAP-Rule:MF_00061};
GN   OrderedLocusNames=Pcar_2005;
OS   Pelobacter carbinolicus (strain DSM 2380 / Gra Bd 1).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Pelobacteraceae; Pelobacter.
OX   NCBI_TaxID=338963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2380 / Gra Bd 1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Pelobacter carbinolicus DSM 2380.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy
CC       group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
CC       {ECO:0000255|HAMAP-Rule:MF_00061}.
CC   -!- CATALYTIC ACTIVITY: ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-
CC       erythritol = ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-
CC       D-erythritol. {ECO:0000255|HAMAP-Rule:MF_00061}.
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
CC       biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
CC       deoxy-D-xylulose 5-phosphate: step 3/6. {ECO:0000255|HAMAP-
CC       Rule:MF_00061}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00061}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000142; ABA89246.1; -; Genomic_DNA.
DR   RefSeq; YP_006717754.1; NC_007498.2.
DR   ProteinModelPortal; Q3A311; -.
DR   STRING; 338963.Pcar_2005; -.
DR   EnsemblBacteria; ABA89246; ABA89246; Pcar_2005.
DR   GeneID; 3724696; -.
DR   KEGG; pca:Pcar_2005; -.
DR   PATRIC; 22890242; VBIPelCar86875_2172.
DR   eggNOG; COG1947; -.
DR   HOGENOM; HOG000019600; -.
DR   KO; K00919; -.
DR   OMA; CVYSETA; -.
DR   OrthoDB; EOG62VNQ2; -.
DR   BioCyc; PCAR338963:GKDU-2219-MONOMER; -.
DR   UniPathway; UPA00056; UER00094.
DR   GO; GO:0050515; F:4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; 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; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.890; -; 1.
DR   HAMAP; MF_00061; IspE; 1.
DR   InterPro; IPR013750; GHMP_kinase_C_dom.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR004424; IspE.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   PANTHER; PTHR20861:SF2; PTHR20861:SF2; 1.
DR   Pfam; PF08544; GHMP_kinases_C; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   PIRSF; PIRSF010376; IspE; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55060; SSF55060; 1.
DR   TIGRFAMs; TIGR00154; ispE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Isoprene biosynthesis; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN         1    280       4-diphosphocytidyl-2-C-methyl-D-
FT                                erythritol kinase.
FT                                /FTId=PRO_0000235112.
FT   NP_BIND      93    103       ATP. {ECO:0000255|HAMAP-Rule:MF_00061}.
FT   ACT_SITE      9      9       {ECO:0000255|HAMAP-Rule:MF_00061}.
FT   ACT_SITE    135    135       {ECO:0000255|HAMAP-Rule:MF_00061}.
SQ   SEQUENCE   280 AA;  30219 MW;  0238777B4F9FFAEF CRC64;
     MESFLAPAKI NICLHVLGRR EDGYHELAML MQRVSLYDRI SLSFIEGNDI RVQCDGLTLP
     LGQKNIAARA AQALFDRAGI RRGLDIVIEK NIPVAAGLGG GSSDAATVLM GLNDMLGLGL
     SATQLMQEGV KLGADVPFFI YKHPAWATGI GDKLQEVEGL PPVWYVLVNP GLEVSTAWVY
     QNLRLTSARD NLRIPRFSGT VDEVVELLHN DLETVTVERF PLIGEIKQQL LGLGARGALM
     SGSGSTVFGV FSDGDTARAA AENLSSRSGW RAFAVEPVND
//
DBGET integrated database retrieval system