(data stored in ACNUC7421 zone)

SWISSPROT: ISPE_THEFY

ID   ISPE_THEFY              Reviewed;         307 AA.
AC   Q47SX2;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 87.
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=Tfu_0407;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX;
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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; CP000088; AAZ54445.1; -; Genomic_DNA.
DR   RefSeq; WP_011290854.1; NC_007333.1.
DR   SMR; Q47SX2; -.
DR   STRING; 269800.Tfu_0407; -.
DR   PRIDE; Q47SX2; -.
DR   EnsemblBacteria; AAZ54445; AAZ54445; Tfu_0407.
DR   KEGG; tfu:Tfu_0407; -.
DR   eggNOG; ENOG4105CTR; Bacteria.
DR   eggNOG; COG1947; LUCA.
DR   HOGENOM; HOG000019600; -.
DR   KO; K00919; -.
DR   OMA; VACDALW; -.
DR   OrthoDB; 1938933at2; -.
DR   BioCyc; TFUS269800:G1G4Q-412-MONOMER; -.
DR   UniPathway; UPA00056; UER00094.
DR   Proteomes; UP000000434; 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; Q47SX2.
DR   SWISS-2DPAGE; Q47SX2.
KW   ATP-binding; Complete proteome; Isoprene biosynthesis; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN         1    307       4-diphosphocytidyl-2-C-methyl-D-
FT                                erythritol kinase.
FT                                /FTId=PRO_0000235147.
FT   NP_BIND     107    117       ATP. {ECO:0000255|HAMAP-Rule:MF_00061}.
FT   ACT_SITE     14     14       {ECO:0000255|HAMAP-Rule:MF_00061}.
FT   ACT_SITE    149    149       {ECO:0000255|HAMAP-Rule:MF_00061}.
SQ   SEQUENCE   307 AA;  31099 MW;  DD48F4C68A0567B3 CRC64;
     MNAPTSVTVR VPAKVNLRLA VGPVRGDGYH GLVNVFHAVS LYDEVTVSPR SDLAPGQAVL
     SVDGERPDHV ARVPLDDSNL AARAAALLAR HVPHATGVHI HVHKAIPVAG GMAGGSADAA
     AALVACDALW EGGTPRERLL ELAAELGSDV AFPLIGCTAV GTGRGEQLSP LPVQGTFHWV
     FALVDGGLST TKVFAEYDRL RPDAPEPTLD DALVAALAAG DARRLGAALT NDLQPAALAL
     RPELGDLLEA GRAAGALGAL VSGSGPTCAF LAESADHARE LAAALRASGT CADTVTAHGP
     VPGATVV
//

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