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Q7NQS8 (ISPE_CHRVO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
Short name=CMK
EC=2.7.1.148
Alternative name(s):
4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase
Gene names
Name:ispE
Ordered Locus Names:CV_4059
OrganismChromobacterium violaceum [Complete proteome] [HAMAP]
Taxonomic identifier536 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Chromobacterium

Protein attributes

Sequence length284 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol By similarity. HAMAP MF_00061

Catalytic activity

ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. HAMAP MF_00061

Pathway

Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6. HAMAP MF_00061

Sequence similarities

Belongs to the GHMP kinase family. IspE subfamily.

Ontologies

Keywords
   Biological processIsoprene biosynthesis
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processterpenoid biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Molecular function4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity

Inferred from electronic annotation. Source: EC

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2842844-diphosphocytidyl-2-C-methyl-D-erythritol kinase HAMAP MF_00061
PRO_0000189206

Regions

Nucleotide binding96 – 10611ATP Potential

Sites

Active site131 By similarity
Active site1381 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NQS8 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 1B8F4436269767A2

FASTA28431,380
        10         20         30         40         50         60 
MQHPFHSYPA PAKLNLLLHV VGKRPDGYHL LETVFRFIDF GDTLELAVRD DGQIVLLTPT 

        70         80         90        100        110        120 
DGVPPEQDLT VRAARLLQRE SGCRLGASIK LEKRTPMGGG LGGGSSDAAT ALIALNRLWG 

       130        140        150        160        170        180 
LAWPRERLQA LGLQLGADVP VFIFGRNALA TGVGEVLEPI PLKPAWYLVI HPQVHVSTIE 

       190        200        210        220        230        240 
VFRNFSQTVL TEIGRVGIMR ILETTQQRRN DLQSVVEKRF PAVNEVLSEL RKYGSPLMTG 

       250        260        270        280 
SGSCVFLEFE SKDEADKVYR VLSQKYQGFV AEGLDVHPLF DSAE

« Hide

References

[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016825 Genomic DNA. Translation: AAQ61719.1.
RefSeqNP_903729.1. NC_005085.1.

3D structure databases

ProteinModelPortalQ7NQS8.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2550097.
GenomeReviewsGene locus CV_4059 in contig AE016825_GR.
KEGGcvi:CV_4059.
NMPDRfig|243365.1.peg.4059.
PATRIC21442927. VBIChrVio67196_3971.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG734593.
OMASSTKEMY.
PhylomeDBQ7NQS8.
ProtClustDBPRK00343.

Enzyme and pathway databases

BioCycCVIO243365:CV_4059-MONOMER.

Family and domain databases

HAMAPMF_00061. IspE.
[Tree]
InterProIPR006204. GHMP_kinase.
IPR013750. GHMP_kinase_C.
IPR004424. IspE.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
Gene3DG3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 1 hit.
KOK00919.
PANTHERPTHR20861:SF2. IspE. 1 hit.
PfamPF08544. GHMP_kinases_C. 1 hit.
PF00288. GHMP_kinases_N. 1 hit.
[Graphical view]
PIRSFPIRSF010376. IspE. 1 hit.
SUPFAMSSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.
TIGRFAMsTIGR00154. IspE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameISPE_CHRVO
AccessionPrimary (citable) accession number: Q7NQS8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: December 15, 2003
Last modified: January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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