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Reviewed, UniProtKB/Swiss-Prot A1VDX6 (ISPDF_DESVV)

Last modified November 3, 2009. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Bifunctional enzyme ispD/ispF
Including the following 2 domains:
    1- Recommended name:
            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- Recommended name:
            2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
                Short name=MECPS
                Short name=MECDP-synthase
              EC=4.6.1.12
Gene names
Name: ispDF
Ordered Locus Names: Dvul_1625
OrganismDesulfovibrio vulgaris subsp. vulgaris (strain DP4) [Complete proteome] [HAMAP]
Taxonomic identifier391774 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length395 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

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 – 395395Bifunctional enzyme ispD/ispF HAMAP MF_01520
PRO_0000296744

Regions

Region1 – 2372372-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
Region238 – 3951582-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520

Sites

Metal binding2441Divalent metal cation By similarity
Metal binding2461Divalent metal cation By similarity
Metal binding2781Divalent metal cation By similarity
Site151Transition state stabilizer By similarity
Site251Transition state stabilizer By similarity
Site1611Positions MEP for the nucleophilic attack By similarity
Site2171Positions MEP for the nucleophilic attack By similarity
Site2701Transition state stabilizer By similarity
Site3691Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
A1VDX6-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: B21D4C2D48587876

FASTA39541,726
        10         20         30         40         50         60 
MRTWVLLLAA GSGTRLATAG LPDAKQFLPL HGAPLYWASA RTMAHVAGIE GIVFVFPPHR 

        70         80         90        100        110        120 
VEEERARISA LDDGSVLGLD WHVVGGGAAR QDSVACGLAA LPRSCEAVLV HDAARPFASP 

       130        140        150        160        170        180 
ALVARVLSAL HDGHAGVVPG IPLTDTVKET TDGFVANTPD RSRLVAVQTP QGFTLKALST 

       190        200        210        220        230        240 
AHETARTAGW NVTDDAALLE RCGIPVRIVA GEVVNAKITT PEDLAMLDAN EPQVTVPCVG 

       250        260        270        280        290        300 
WGYDVHRYGE GRPMKLGGVL IPEGPEVVAH SDGDVLLHAL ADALLGCIGA GDIGLHFPDS 

       310        320        330        340        350        360 
DAAFDNANSA MLLDRVLHMT HEARLRLTHV DLTIVAQVPK LSPWRDKIRA NVARLLDLPV 

       370        380        390 
TSVNFKATTE EGLGFTGEKR GIKAIAAVTG LRPMP 

« Hide

References

[1]"Complete sequence of chromosome 1 of Desulfovibrio vulgaris subsp. vulgaris DP4."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Lykidis A., Walker C., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000527 Genomic DNA. Translation: ABM28642.1.
RefSeqYP_967069.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA1VDX6.

Genome annotation databases

GeneID4664257.
GenomeReviewsGene locus Dvul_1625 in contig CP000527_GR.
KEGGdvl:Dvul_1625.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAIVLIHDA.

Family and domain databases

HAMAPMF_01520.
[Tree]
InterProIPR001228. ISPD_synthase.
IPR018294. ISPD_synthase_CS.
IPR003526. MECDP_synthase_core.
IPR020555. MECDP_synthase_CS.
[Graphical view]
Gene3DG3DSA:3.30.1330.50. MECDP_synthase_core. 1 hit.
PfamPF01128. IspD. 1 hit.
PF02542. YgbB. 1 hit.
[Graphical view]
TIGRFAMsTIGR00453. ispD. 1 hit.
TIGR00151. ispF. 1 hit.
PROSITEPS01295. ISPD. 1 hit.
PS01350. ISPF. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameISPDF_DESVV
AccessionPrimary (citable) accession number: A1VDX6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: February 6, 2007
Last modified: November 3, 2009
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents