(data stored in SCRATCH zone)

SWISSPROT: C6B2P9_RHILS

ID   C6B2P9_RHILS            Unreviewed;       303 AA.
AC   C6B2P9;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 65.
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=Rleg_0565 {ECO:0000313|EMBL:ACS54869.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54869.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54869.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54869.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy
CC       group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
CC       {ECO:0000256|HAMAP-Rule:MF_00061, ECO:0000256|SAAS:SAAS00651852}.
CC   -!- CATALYTIC ACTIVITY: ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-
CC       erythritol = ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-
CC       D-erythritol. {ECO:0000256|HAMAP-Rule:MF_00061,
CC       ECO:0000256|SAAS:SAAS00651860}.
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:0000256|HAMAP-
CC       Rule:MF_00061}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00061, ECO:0000256|SAAS:SAAS00651857}.
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DR   EMBL; CP001622; ACS54869.1; -; Genomic_DNA.
DR   RefSeq; WP_012756249.1; NC_012850.1.
DR   ProteinModelPortal; C6B2P9; -.
DR   EnsemblBacteria; ACS54869; ACS54869; Rleg_0565.
DR   KEGG; rlg:Rleg_0565; -.
DR   HOGENOM; HOG000019600; -.
DR   KO; K00919; -.
DR   OMA; RWPSPAK; -.
DR   OrthoDB; POG091H00XD; -.
DR   UniPathway; UPA00056; UER00094.
DR   Proteomes; UP000002256; Chromosome.
DR   GO; GO:0050515; F:4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
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-HAMAP.
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; 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; C6B2P9.
DR   SWISS-2DPAGE; C6B2P9.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00061,
KW   ECO:0000256|SAAS:SAAS00651866};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00061};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00061,
KW   ECO:0000256|SAAS:SAAS00651834, ECO:0000313|EMBL:ACS54869.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00061,
KW   ECO:0000256|SAAS:SAAS00651849};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00061,
KW   ECO:0000256|SAAS:SAAS00651864}.
FT   DOMAIN      103    158       GHMP_kinases_N. {ECO:0000259|Pfam:
FT                                PF00288}.
FT   DOMAIN      220    284       GHMP_kinases_C. {ECO:0000259|Pfam:
FT                                PF08544}.
FT   NP_BIND     111    121       ATP. {ECO:0000256|HAMAP-Rule:MF_00061}.
FT   ACT_SITE     24     24       {ECO:0000256|HAMAP-Rule:MF_00061}.
FT   ACT_SITE    153    153       {ECO:0000256|HAMAP-Rule:MF_00061}.
SQ   SEQUENCE   303 AA;  31700 MW;  390DA021DCCC7B4B CRC64;
     MMSSENRSHF SASCSSFSEE ARAKINLALH VTGQRPDGYH LLDMLVTFAD HGDRLDFMRS
     PTDALTLSGR FGETLAGDGG TNLVLKARDL LREVVGPLAF PVRIHLEKNL PIASGIGGGS
     ADAAATLRGL MRLWGTTLSA ETLAALALKL GADVPMCLES RPLIARGIGE KIEPVPDLPA
     FAMVLANPLK GVATPEVFRR LATKNNPALS LALSGSQAAD WLAAIAAARN DLEPPARGLV
     PEIAAISAML QARGALLTRM SGSGATCFGI FASMTAAEGA AAALHDKRPD WYFQATETVS
     GGA
//

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