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Q310X3 (ISPDF_DESDG) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. 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:
Bifunctional enzyme IspD/IspF

Including the following 2 domains:

  1. 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
    EC=2.7.7.60
    Alternative name(s):
    4-diphosphocytidyl-2C-methyl-D-erythritol synthase
    MEP cytidylyltransferase
    Short name=MCT
  2. 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
    Short name=MECDP-synthase
    Short name=MECPS
    EC=4.6.1.12
Gene names
Name:ispDF
Ordered Locus Names:Dde_1726
OrganismDesulfovibrio desulfuricans (strain G20) [Complete proteome] [HAMAP]
Taxonomic identifier207559 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length399 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and converts 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate into 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (MECDP) and CMP (IspF) By similarity. HAMAP MF_01520

Catalytic activity

CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. HAMAP MF_01520

2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + CMP. HAMAP MF_01520

Cofactor

Divalent metal cations By similarity. HAMAP MF_01520

Pathway

Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6. HAMAP MF_01520

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

Sequence similarities

In the N-terminal section; belongs to the IspD family.

In the C-terminal section; belongs to the IspF family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 399399Bifunctional enzyme IspD/IspF HAMAP MF_01520
PRO_0000296743

Regions

Region1 – 2392392-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
Region240 – 3991602-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520

Sites

Metal binding2461Divalent metal cation By similarity
Metal binding2481Divalent metal cation By similarity
Metal binding2811Divalent metal cation By similarity
Site151Transition state stabilizer By similarity
Site251Transition state stabilizer By similarity
Site1611Positions MEP for the nucleophilic attack By similarity
Site2181Positions MEP for the nucleophilic attack By similarity
Site2731Transition state stabilizer By similarity
Site3721Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q310X3 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 1B92A1B5A5F79DA4

FASTA39942,461
        10         20         30         40         50         60 
MHTWALLLAA GQSSRIAAAC PGVRKQFLLW QNAPLFWHSA VMLSRVSRMR GIIFVFPEDM 

        70         80         90        100        110        120 
LEEATAMVRE LDAGRALGIP WKAVSGGARR QDSVASGLGQ LPAECDTVLV HDAARPFASA 

       130        140        150        160        170        180 
SLTNSILDAL QAGAEGVVPA LAVTDTIKVV EDGAVLSTPD RTKLVAVQTP QGFSLQALLG 

       190        200        210        220        230        240 
AHRHCAEKAL AVTDDASMLE LLGQHTVITV EGEASNIKVT HPEDLTMLHS SEKKNMQVPC 

       250        260        270        280        290        300 
VGWGYDVHRF GSDGRPMKLG GVPIAGGPGV IAHSDGDVLL HALTDAVLGC MGLGDIGMLF 

       310        320        330        340        350        360 
PDTDAAYDNA DSAVMLNEVL EKARNAGLLI THVDLTIITQ IPRITPWRDQ IHKNICRITR 

       370        380        390 
LDASSVNLKA TTEEKLGFTG EKKGIKAVAA VTALRRVSS 

« Hide

References

[1]"Complete sequence of Desulfovibrio desulfuricans G20."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goodwin L.A., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: G20.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000112 Genomic DNA. Translation: ABB38523.1.
RefSeqYP_388218.1. NC_007519.1.

3D structure databases

HSSPHSSP built from PDB template 1H47 based on UniProtKB P62617.
ProteinModelPortalQ310X3.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ310X3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3756724.
GenomeReviewsGene locus Dde_1726 in contig CP000112_GR.
KEGGdde:Dde_1726.
NMPDRfig|207559.3.peg.1539.
PATRIC21742409. VBIDesDes50040_1723.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1211.
HOGENOMHBG672839.
OMAIVLIHDA.
ProtClustDBCLSK705254.

Enzyme and pathway databases

BioCycDDES207559:DDE_1726-MONOMER.

Family and domain databases

HAMAPMF_01520. IspDF.
[Tree]
InterProIPR023423. IpsF_dom.
IPR001228. ISPD_synthase.
IPR018294. ISPD_synthase_CS.
IPR003526. MECDP_synthase.
IPR020555. MECDP_synthase_CS.
[Graphical view]
Gene3DG3DSA:3.30.1330.50. MECDP_synthase_core. 1 hit.
KOK12506.
PfamPF01128. IspD. 1 hit.
PF02542. YgbB. 1 hit.
[Graphical view]
SUPFAMSSF69765. YgbB_synth. 1 hit.
TIGRFAMsTIGR00453. IspD. 1 hit.
TIGR00151. IspF. 1 hit.
PROSITEPS01295. ISPD. 1 hit.
PS01350. ISPF. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameISPDF_DESDG
AccessionPrimary (citable) accession number: Q310X3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: December 6, 2005
Last modified: January 25, 2012
This is version 47 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