(data stored in ACNUC7421 zone)

SWISSPROT: ISPE_PARXL

ID   ISPE_PARXL              Reviewed;         293 AA.
AC   Q145X1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 78.
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=Bxeno_A0330; ORFNames=Bxe_A4132;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000270; ABE28868.1; -; Genomic_DNA.
DR   RefSeq; WP_011486699.1; NZ_CP008760.1.
DR   SMR; Q145X1; -.
DR   STRING; 266265.Bxe_A4132; -.
DR   PRIDE; Q145X1; -.
DR   EnsemblBacteria; ABE28868; ABE28868; Bxe_A4132.
DR   GeneID; 4003430; -.
DR   KEGG; bxb:DR64_1808; -.
DR   KEGG; bxe:Bxe_A4132; -.
DR   PATRIC; fig|266265.5.peg.350; -.
DR   eggNOG; ENOG4105CTR; Bacteria.
DR   eggNOG; COG1947; LUCA.
DR   HOGENOM; HOG000019601; -.
DR   KO; K00919; -.
DR   OMA; RWPSPAK; -.
DR   OrthoDB; 1938933at2; -.
DR   BioCyc; BXEN266265:BXE_RS01655-MONOMER; -.
DR   UniPathway; UPA00056; UER00094.
DR   Proteomes; UP000001817; Chromosome 1.
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   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;
DR   PRODOM; Q145X1.
DR   SWISS-2DPAGE; Q145X1.
KW   ATP-binding; Complete proteome; Isoprene biosynthesis; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN         1    293       4-diphosphocytidyl-2-C-methyl-D-
FT                                erythritol kinase.
FT                                /FTId=PRO_1000007826.
FT   NP_BIND      99    109       ATP. {ECO:0000255|HAMAP-Rule:MF_00061}.
FT   ACT_SITE     16     16       {ECO:0000255|HAMAP-Rule:MF_00061}.
FT   ACT_SITE    141    141       {ECO:0000255|HAMAP-Rule:MF_00061}.
SQ   SEQUENCE   293 AA;  32021 MW;  EAED96091AE19A41 CRC64;
     MIETTDSLRD CLAPAKLNLF LHITGRRPDG YHTLQTVFQL LDWGDTLHFT RRDDGLITRR
     TEIADVPPEH DLTVRAATLL KTHTGSPEGV DIEIDKRLPM GAGLGGGSSN AATTLLALNR
     LWKLNLPRLE LQALALKLGA DVPFFVFGKN AFAQGVGEAL DVVQLPPRHF LVVTPRVHVP
     TAAIFSEKAL TRDSKPLTIT DFPAELSCNT EWPESFGRND MQQVVVGKYA EVAQVLRWFE
     NVAPARMSGS GASVFAAFRS KAEAEAVQAK LPAEWNSAVA ASLDQHPLFT FAS
//

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