(data stored in SCRATCH9089 zone)

SWISSPROT: ISPE_PASMU

ID   ISPE_PASMU              Reviewed;         295 AA.
AC   P57833;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   11-DEC-2019, entry version 112.
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}; OrderedLocusNames=PM0245;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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}.
DR   EMBL; AE004439; AAK02329.1; -; Genomic_DNA.
DR   RefSeq; WP_005724298.1; NC_002663.1.
DR   SMR; P57833; -.
DR   EnsemblBacteria; AAK02329; AAK02329; PM0245.
DR   KEGG; pmu:PM0245; -.
DR   PATRIC; fig|272843.6.peg.253; -.
DR   eggNOG; ENOG4105CTR; Bacteria.
DR   eggNOG; COG1947; LUCA.
DR   HOGENOM; HOG000019601; -.
DR   KO; K00919; -.
DR   OMA; RWPSPAK; -.
DR   BioCyc; PMUL272843:G1FZ8-256-MONOMER; -.
DR   UniPathway; UPA00056; UER00094.
DR   Proteomes; UP000000809; 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   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; P57833.
DR   SWISS-2DPAGE; P57833.
KW   ATP-binding; Isoprene biosynthesis; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..295
FT                   /note="4-diphosphocytidyl-2-C-methyl-D-erythritol kinase"
FT                   /id="PRO_0000189242"
FT   NP_BIND         108..118
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
FT   ACT_SITE        25
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
FT   ACT_SITE        150
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
SQ   SEQUENCE   295 AA;  33064 MW;  5FE9FEB7C9ABDA55 CRC64;
     MQHYHFSHSL LAQQEKPYRF PCPAKLNLFL YINGKRQDGY HELQTLFQFV DFGDWLDIEV
     REDNEICLTP ELPSLKNEDN LVYRAAKLLQ QKTNCALGAN LTLDKILPMG SGLGGGSSNA
     ATALVALNYL WNTQLSTKQL AKLGLMLGAD VPIFVHGHAA FAEGVGEKIT YCEPKEKWYV
     VLKPNVSIST ATVFSDPDLI RNTPKQSLEQ LLNQKYANDC EKVVLNHYPE VEEILHRLLQ
     YAPSRLTGTG ACVFAEFNDE ESAQLAFQTI PKNYFGFVAQ GLNKSPLHNM LAKIS
//

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