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Q72C30 (ISPDF_DESVH) 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:
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
Synonyms:ispD
Ordered Locus Names:DVU_1454
OrganismDesulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Taxonomic identifier882 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Desulfovibrionales › Desulfovibrionaceae › Desulfovibrio

Protein attributes

Sequence length395 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 – 395395Bifunctional enzyme IspD/IspF HAMAP MF_01520
PRO_0000075666

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
Q72C30 [UniParc].

Last modified July 5, 2004. 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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017285 Genomic DNA. Translation: AAS95932.1.
RefSeqYP_010673.1. NC_002937.3.

3D structure databases

ProteinModelPortalQ72C30.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ72C30.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2794820.
GenomeReviewsGene locus DVU_1454 in contig AE017285_GR.
KEGGdvu:DVU1454.
PATRIC32062740. VBIDesVul119526_1353.
TIGRDVU_1454.

Phylogenomic databases

eggNOGCOG1211.
HOGENOMHBG672839.
OMAIVLIHDA.
PhylomeDBQ72C30.
ProtClustDBCLSK705254.

Enzyme and pathway databases

BioCycDVUL882:DVU_1454-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_DESVH
AccessionPrimary (citable) accession number: Q72C30
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: July 5, 2004
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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