ISPE_GRABC
ID ISPE_GRABC Reviewed; 302 AA.
AC Q0BR06;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=GbCGDNIH1_1848;
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Granulibacter.
OX NCBI_TaxID=391165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1260 / CGDNIH1;
RX PubMed=17827295; DOI=10.1128/jb.00793-07;
RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT "Genome sequence analysis of the emerging human pathogenic acetic acid
RT bacterium Granulibacter bethesdensis.";
RL J. Bacteriol. 189:8727-8736(2007).
CC -!- FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group
CC of 4-diphosphocytidyl-2C-methyl-D-erythritol. {ECO:0000255|HAMAP-
CC 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 biosynthesis
CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC phosphate: step 3/6. {ECO:0000255|HAMAP-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; CP000394; ABI62746.1; -; Genomic_DNA.
DR RefSeq; WP_011632548.1; NC_008343.2.
DR AlphaFoldDB; Q0BR06; -.
DR SMR; Q0BR06; -.
DR STRING; 391165.GbCGDNIH1_1848; -.
DR EnsemblBacteria; ABI62746; ABI62746; GbCGDNIH1_1848.
DR KEGG; gbe:GbCGDNIH1_1848; -.
DR eggNOG; COG1947; Bacteria.
DR HOGENOM; CLU_053057_1_0_5; -.
DR OMA; RWPSPAK; -.
DR UniPathway; UPA00056; UER00094.
DR Proteomes; UP000001963; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 PANTHER; PTHR43527:SF2; PTHR43527: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; Isoprene biosynthesis; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..302
FT /note="4-diphosphocytidyl-2-C-methyl-D-erythritol kinase"
FT /id="PRO_0000335716"
FT ACT_SITE 13
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
FT ACT_SITE 143
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
FT BINDING 101..111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
SQ SEQUENCE 302 AA; 31914 MW; 550CCC3DEBFBFF08 CRC64;
MIVDQNVAFA PAKINLYLHV TGRRSDGYHL LDSLAVFAEA CDVLRYRDGD QAAGLGLQLE
GPGAETLRAE PDNLVLRAGR ALAALAGIKP RGTIMLDKRL PVASGIGGGS SDAAAALRLL
SRVWGVSPAA EDLHRIATSL GADVPVCLEP GTYRMRGIGE RLEALPAMPE IGLLLANPGV
PVSTPEVFRN REHGFTPEAT LASRWPDMAA LLRDLQLSRN DLQPPAMRLC PAIGILLHAL
EGLPGARLTR MSGSGATCFT LFDHPDAARD AAQLLQAQSG MGGWCWGGGL YKTASALDKT
TL