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Database: UniProt/SWISS-PROT
Entry: ISPE_EUBE2
LinkDB: ISPE_EUBE2
Original site: ISPE_EUBE2 
ID   ISPE_EUBE2              Reviewed;         288 AA.
AC   C4Z205;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   29-OCT-2014, entry version 38.
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=EUBELI_00159;
OS   Eubacterium eligens (strain ATCC 27750 / VPI C15-48).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=515620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27750 / VPI C15-48;
RX   PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA   Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA   Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA   Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA   Hettich R.L., Gordon J.I.;
RT   "Characterizing a model human gut microbiota composed of members of
RT   its two dominant bacterial phyla.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
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}.
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DR   EMBL; CP001104; ACR71195.1; -; Genomic_DNA.
DR   RefSeq; YP_002929642.1; NC_012778.1.
DR   ProteinModelPortal; C4Z205; -.
DR   STRING; 515620.EUBELI_00159; -.
DR   EnsemblBacteria; ACR71195; ACR71195; EUBELI_00159.
DR   GeneID; 7958324; -.
DR   KEGG; eel:EUBELI_00159; -.
DR   PATRIC; 21863518; VBIEubEli113401_0146.
DR   eggNOG; COG1947; -.
DR   HOGENOM; HOG000019600; -.
DR   KO; K00919; -.
DR   OMA; YHEIRTI; -.
DR   OrthoDB; EOG62VNQ2; -.
DR   BioCyc; EELI515620:GH1N-159-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    288       4-diphosphocytidyl-2-C-methyl-D-
FT                                erythritol kinase.
FT                                /FTId=PRO_1000202379.
FT   NP_BIND      95    105       ATP. {ECO:0000255|HAMAP-Rule:MF_00061}.
FT   ACT_SITE     11     11       {ECO:0000255|HAMAP-Rule:MF_00061}.
FT   ACT_SITE    137    137       {ECO:0000255|HAMAP-Rule:MF_00061}.
SQ   SEQUENCE   288 AA;  31946 MW;  37792CED3103805D CRC64;
     MESIRLKARA KINLGLDVIG RRENGYHDVR MVMQTVGLYD RIIMTRIPEE EIRIKTNIGF
     LPVNENNLVY KAIMLMKNKY KLDGGIEVDL NKFIPVAAGM AGGSSDAACA LFGMNRLFEL
     NVPMRELMKL GVEIGADVPY CLMRGTALAE GIGEKLTRLP DMPFCHILIA KPPVNVSTKL
     VYEKLDNTDV KLHPDIDGII EAIKLKDVAL VASRMGNVLE SVTIPLYPVI DSIKKDMIEH
     GAINAMMSGS GPTVFGIFPD EQSMIACQQF LRQKGEARQV YTTETFTP
//
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