(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BHJ7_GEOS0

ID   A0A0F6BHJ7_GEOS0        Unreviewed;       289 AA.
AC   A0A0F6BHJ7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 30.
DE   RecName: Full=4-diphosphocytidyl-2-C-methyl-D-erythritol kinase {ECO:0000256|HAMAP-Rule:MF_00061};
DE            Short=CMK {ECO:0000256|HAMAP-Rule:MF_00061};
DE            EC=2.7.1.148 {ECO:0000256|HAMAP-Rule:MF_00061};
DE   AltName: Full=4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase {ECO:0000256|HAMAP-Rule:MF_00061};
GN   Name=ispE {ECO:0000256|HAMAP-Rule:MF_00061};
GN   OrderedLocusNames=GY4MC1_0042 {ECO:0000313|EMBL:ADP72898.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72898.1};
RN   [1] {ECO:0000313|EMBL:ADP72898.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72898.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group
CC       of 4-diphosphocytidyl-2C-methyl-D-erythritol. {ECO:0000256|HAMAP-
CC       Rule:MF_00061, ECO:0000256|SAAS:SAAS01090930}.
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:0000256|HAMAP-Rule:MF_00061,
CC         ECO:0000256|SAAS:SAAS01124723};
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:0000256|HAMAP-Rule:MF_00061}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00061, ECO:0000256|SAAS:SAAS00571601}.
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DR   EMBL; CP002293; ADP72898.1; -; Genomic_DNA.
DR   RefSeq; WP_003247408.1; NC_014650.1.
DR   EnsemblBacteria; ADP72898; ADP72898; GY4MC1_0042.
DR   GeneID; 29237337; -.
DR   KEGG; gmc:GY4MC1_0042; -.
DR   KO; K00919; -.
DR   OMA; RWPSPAK; -.
DR   OrthoDB; 1938933at2; -.
DR   BioCyc; GSP581103:G1GOQ-53-MONOMER; -.
DR   UniPathway; UPA00056; UER00094.
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; A0A0F6BHJ7.
DR   SWISS-2DPAGE; A0A0F6BHJ7.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00061,
KW   ECO:0000256|SAAS:SAAS00462204};
KW   Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00061};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00061, ECO:0000256|SAAS:SAAS00462177,
KW   ECO:0000313|EMBL:ADP72898.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00061,
KW   ECO:0000256|SAAS:SAAS00090324};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00061,
KW   ECO:0000256|SAAS:SAAS00462229}.
FT   DOMAIN          87..144
FT                   /note="GHMP_kinases_N"
FT                   /evidence="ECO:0000259|Pfam:PF00288"
FT   DOMAIN          197..271
FT                   /note="GHMP_kinases_C"
FT                   /evidence="ECO:0000259|Pfam:PF08544"
FT   NP_BIND         94..104
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00061"
FT   ACT_SITE        10
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00061"
FT   ACT_SITE        136
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00061"
SQ   SEQUENCE   289 AA;  31402 MW;  1050CBCC9831DFC1 CRC64;
     MKVLVKAPAK INLSLDVLHK RPDGYHEVKM VMTTIDLADR IELIPRTDDV IQIISQNRFV
     PDDHRNLAYQ AAKVLKDTFG IKQGVAISIT KNIPVAAGLA GGSSDAAATL RGLNKLWRLG
     LTLDELAELG AQIGSDVPFC VYGGTAVATG RGEKIMPISS PPPCWVILAK PSIGVSTAEV
     YRNLKVGEIQ HPDVDGMVEA IERQDYAAIC QLVGNVLEEV TLKMHPEVAH IKEQMKRFGA
     DAVLMSGSGP TVFGLVQHDS RLQRIYNGLR GFCDQVFAVR ILGEQNSLD
//

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