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 29-MAY-2013, entry version 51.
DE RecName: Full=4-diphosphocytidyl-2-C-methyl-D-erythritol kinase;
DE Short=CMK;
DE EC=2.7.1.148;
DE AltName: Full=4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase;
GN Name=ispE; 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 (By
CC similarity).
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.
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
CC deoxy-D-xylulose 5-phosphate: step 3/6.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily.
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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 ProtClustDB; PRK14614; -.
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:HAMAP.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, mevalonate-independent pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.30.230.10; -; 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; Ribosomal_S5_D2-typ_fold; 1.
DR TIGRFAMs; TIGR00154; ispE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Isoprene biosynthesis; Kinase;
KW Nucleotide-binding; Transferase.
FT CHAIN 1 280 4-diphosphocytidyl-2-C-methyl-D-
FT erythritol kinase.
FT /FTId=PRO_0000235112.
FT NP_BIND 93 103 ATP (Potential).
FT ACT_SITE 9 9 By similarity.
FT ACT_SITE 135 135 By similarity.
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
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