(data stored in ACNUC7421 zone)

SWISSPROT: ISPE_ANADE

ID   ISPE_ANADE              Reviewed;         313 AA.
AC   Q2IM67;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 72.
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=Adeh_0123;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) 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:
CC       Reaction=4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-
CC         erythritol 2-phosphate + ADP + H(+); Xref=Rhea:RHEA:18437,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57823,
CC         ChEBI:CHEBI:57919, ChEBI:CHEBI:456216; EC=2.7.1.148;
CC         Evidence={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}.
DR   EMBL; CP000251; ABC79900.1; -; Genomic_DNA.
DR   RefSeq; WP_011419183.1; NC_007760.1.
DR   SMR; Q2IM67; -.
DR   STRING; 290397.Adeh_0123; -.
DR   EnsemblBacteria; ABC79900; ABC79900; Adeh_0123.
DR   KEGG; ade:Adeh_0123; -.
DR   eggNOG; ENOG4107Z7S; Bacteria.
DR   eggNOG; COG1947; LUCA.
DR   HOGENOM; HOG000019600; -.
DR   KO; K00919; -.
DR   OMA; RWPSPAK; -.
DR   BioCyc; ADEH290397:G1G5W-127-MONOMER; -.
DR   UniPathway; UPA00056; UER00094.
DR   Proteomes; UP000001935; Chromosome.
DR   GO; GO:0050515; F:4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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   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; IPR036554; GHMP_kinase_C_sf.
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   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;
DR   PRODOM; Q2IM67.
DR   SWISS-2DPAGE; Q2IM67.
KW   ATP-binding; Complete proteome; Isoprene biosynthesis; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN         1    313       4-diphosphocytidyl-2-C-methyl-D-
FT                                erythritol kinase.
FT                                /FTId=PRO_0000235059.
FT   NP_BIND      95    105       ATP. {ECO:0000255|HAMAP-Rule:MF_00061}.
FT   ACT_SITE     10     10       {ECO:0000255|HAMAP-Rule:MF_00061}.
FT   ACT_SITE    136    136       {ECO:0000255|HAMAP-Rule:MF_00061}.
SQ   SEQUENCE   313 AA;  32912 MW;  D2ACAA4F4E82B56A CRC64;
     MRLVTLAPAK VNLVLRVGPV RADGYHDLRT LMVPLDLGDR VDVRVSARRG PVRCTVPGRP
     ELHGPENLAA RAAEAFRRRF GVDRAVSIRI EKRTPVTAGL GGGSSDAAAV LRCLARAFRV
     RDRAALAALA LEIGSDVPFF LGPGPAWAAG RGERLSPADV PPLDLVLVYP ADPSLAIRAG
     DAYRWLDEAR AGGPQAPRRL GRPGRWRPSL LGNDLQAPCV ARKPALQALL GLLVGAGATA
     AIMSGSGPTV FGVFPGRGAA RGAALAIQGR AKGGAAGVQV LLARTVRRHP RVSPWRSPRS
     ASSPSTRRSS RPT
//

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