Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q7MVU8 (ISPE_PORGI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:PG_0935
OrganismPorphyromonas gingivalis (strain ATCC BAA-308 / W83) [Complete proteome] [HAMAP]
Taxonomic identifier242619 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Porphyromonadaceae › Porphyromonas

Protein attributes

Sequence length274 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 – 2742744-diphosphocytidyl-2-C-methyl-D-erythritol kinase HAMAP MF_00061
PRO_0000189245

Regions

Nucleotide binding92 – 10211ATP Potential

Sites

Active site81 By similarity
Active site1341 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7MVU8 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 8723EE78E47DCA5E

FASTA27430,237
        10         20         30         40         50         60 
MIVFPNAKIN LGLQVVAKRA DGYHNIETVF YPIPLTDALE IEVREDTCDR LSVHGVPIDA 

        70         80         90        100        110        120 
ATEDNLVMKA VMALRRKFDF PPLTIELIKH IPSGAGLGGG SSNASFMLKL VRDYFSLPID 

       130        140        150        160        170        180 
DEELAAIALT IGADCPFFVG NRPVLATDLG QVFTPLPNFS LSGLHIAIVK PPIHINTAAA 

       190        200        210        220        230        240 
YKGLKHVGKR ETMPDEIVYM PVEEWRGKLV NDFEESLFPE HPRLAELKEM LYRSGALYAA 

       250        260        270 
MSGSGSALFG LFREKPQLDK AAITDCFRWQ SIIP

« Hide

References

[1]"Complete genome sequence of the oral pathogenic bacterium Porphyromonas gingivalis strain W83."
Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E., Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J., Granger D., Tettelin H. expand/collapse author list , Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E., Fraser C.M.
J. Bacteriol. 185:5591-5601(2003) [PubMed: 12949112] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-308 / W83.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE015924 Genomic DNA. Translation: AAQ66069.1.
RefSeqNP_905170.1. NC_002950.2.

3D structure databases

ProteinModelPortalQ7MVU8.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2552951.
GenomeReviewsGene locus PG_0935 in contig AE015924_GR.
KEGGpgi:PG0935.
NMPDRfig|242619.1.peg.811.
PATRIC22978928. VBIPorGin134034_0862.
TIGRPG_0935.

Phylogenomic databases

HOGENOMHBG734593.
OMAVSTAEVY.
PhylomeDBQ7MVU8.
ProtClustDBPRK14609.

Enzyme and pathway databases

BioCycPGIN242619:PG_0935-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_PORGI
AccessionPrimary (citable) accession number: Q7MVU8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: December 15, 2003
Last modified: January 25, 2012
This is version 57 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents