(data stored in SCRATCH zone)

SWISSPROT: C3MHC4_SINFN

ID   C3MHC4_SINFN            Unreviewed;       322 AA.
AC   C3MHC4;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 67.
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   ECO:0000313|EMBL:ACP24252.1};
GN   OrderedLocusNames=NGR_c04560 {ECO:0000313|EMBL:ACP24252.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24252.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24252.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001389; ACP24252.1; -; Genomic_DNA.
DR   RefSeq; WP_012707037.1; NC_012587.1.
DR   RefSeq; YP_002825005.1; NC_012587.1.
DR   ProteinModelPortal; C3MHC4; -.
DR   STRING; 394.NGR_c04560; -.
DR   EnsemblBacteria; ACP24252; ACP24252; NGR_c04560.
DR   GeneID; 7791682; -.
DR   KEGG; rhi:NGR_c04560; -.
DR   PATRIC; fig|394.7.peg.3263; -.
DR   eggNOG; ENOG4105CTR; Bacteria.
DR   eggNOG; COG1947; LUCA.
DR   HOGENOM; HOG000019600; -.
DR   KO; K00919; -.
DR   OMA; RWPSPAK; -.
DR   OrthoDB; POG091H00XD; -.
DR   UniPathway; UPA00056; UER00094.
DR   Proteomes; UP000001054; 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; C3MHC4.
DR   SWISS-2DPAGE; C3MHC4.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00061,
KW   ECO:0000256|SAAS:SAAS00651866};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
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:ACP24252.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00061,
KW   ECO:0000256|SAAS:SAAS00651849};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00061,
KW   ECO:0000256|SAAS:SAAS00651864, ECO:0000313|EMBL:ACP24252.1}.
FT   DOMAIN      122    177       GHMP_kinases_N. {ECO:0000259|Pfam:
FT                                PF00288}.
FT   DOMAIN      243    305       GHMP_kinases_C. {ECO:0000259|Pfam:
FT                                PF08544}.
FT   NP_BIND     130    140       ATP. {ECO:0000256|HAMAP-Rule:MF_00061}.
FT   ACT_SITE     37     37       {ECO:0000256|HAMAP-Rule:MF_00061}.
FT   ACT_SITE    172    172       {ECO:0000256|HAMAP-Rule:MF_00061}.
SQ   SEQUENCE   322 AA;  33938 MW;  8FD5B9143020A131 CRC64;
     MPRRRCRRSP PRRTRNPDSM PADGIAGFAL TLAAPAKINL ALHVVGQRAD GHHLLESLVT
     FAECGDRIAF APADADHFTV SGPFSRDLPV SADGKSGNLV LRARDLLRRE LIGRGAPTTS
     VHLHLEKNLP IASGIGGGSA DAAATLRGLL SLWKAEIAPE RLASLALELG ADVPMCLDGR
     PLLARGIGEE IAPLADLPSF AIVLVNPLVA VSTPVIFRML AEKRNPPLAL PHGAHTAAAW
     LAALADMRND LERPARALEP AVETVSDALQ AVRADLVRMS GSGATCFGLF DSDEKAGAAA
     QRISADQPGW YVLATRTAGK RG
//

If you have problems or comments...

PBIL Back to PBIL home page