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A4TPZ8 (ISPF_YERPP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. 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

Names and origin

Protein namesRecommended name:
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase

Short name=MECDP-synthase
Short name=MECPP-synthase
Short name=MECPS
EC=4.6.1.12
Gene names
Name:ispF
Ordered Locus Names:YPDSF_3000
OrganismYersinia pestis (strain Pestoides F) [Complete proteome] [HAMAP]
Taxonomic identifier386656 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length162 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) By similarity. HAMAP-Rule MF_00107

Catalytic activity

2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + CMP. HAMAP-Rule MF_00107

Cofactor

Binds 1 divalent metal cation per subunit By similarity.

Pathway

Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6. HAMAP-Rule MF_00107

Subunit structure

Homotrimer By similarity. HAMAP-Rule MF_00107

Sequence similarities

Belongs to the IspF family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1621622-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP-Rule MF_00107
PRO_1000022895

Regions

Region8 – 103Substrate binding By similarity
Region36 – 372Substrate binding By similarity
Region40 – 489Substrate binding By similarity
Region58 – 603Substrate binding By similarity
Region63 – 675Substrate binding By similarity
Region102 – 1087Substrate binding By similarity
Region133 – 1375Substrate binding By similarity

Sites

Metal binding81Divalent metal cation By similarity
Metal binding101Divalent metal cation By similarity
Metal binding441Divalent metal cation By similarity
Binding site671Substrate; via carbonyl oxygen By similarity
Binding site1411Substrate; via carbonyl oxygen By similarity
Binding site1441Substrate By similarity
Site361Transition state stabilizer By similarity
Site1351Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
A4TPZ8 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 9A295411D3DFB1EB

FASTA16217,182
        10         20         30         40         50         60 
MRIGHGFDVH KFGENGSGPL IIGGVRIPYE KGLLAHSDGD VALHAATDAL LGAAALGDIG 

        70         80         90        100        110        120 
KLFPDTDPAF KGADSRGLLR EAYRRILAKG YKLGNLDITI IAQAPKMAPH IPQMRVNLAE 

       130        140        150        160 
DLQCHMDDIN VKATTTEQLG FTGRGEGIAC EAVVLLVNVE QG 

« Hide

References

[1]"Complete sequence of chromosome of Yersinia pestis Pestoides F."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Di Bartolo G., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Worsham P., Chu M., Bearden S., Garcia E., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pestoides F.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000668 Genomic DNA. Translation: ABP41360.1.
RefSeqYP_001164333.1. NC_009381.1.

3D structure databases

ProteinModelPortalA4TPZ8.
SMRA4TPZ8. Positions 1-157.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING386656.YPDSF_3000.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP41360; ABP41360; YPDSF_3000.
GeneID5062891.
KEGGypp:YPDSF_3000.
PATRIC18615821. VBIYerPes122972_3789.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0245.
HOGENOMHOG000239175.
KOK01770.
OMAKGYQLGN.
OrthoDBEOG6J48RZ.

Enzyme and pathway databases

BioCycYPES386656:GKD7-3063-MONOMER.
UniPathwayUPA00056; UER00095.

Family and domain databases

Gene3D3.30.1330.50. 1 hit.
HAMAPMF_00107. IspF.
InterProIPR003526. MECDP_synthase.
IPR020555. MECDP_synthase_CS.
[Graphical view]
PfamPF02542. YgbB. 1 hit.
[Graphical view]
SUPFAMSSF69765. SSF69765. 1 hit.
TIGRFAMsTIGR00151. ispF. 1 hit.
PROSITEPS01350. ISPF. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameISPF_YERPP
AccessionPrimary (citable) accession number: A4TPZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 15, 2007
Last modified: May 14, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways