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Q7VFU3 (ISPDF_HELHP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. 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:HH_1582
OrganismHelicobacter hepaticus (strain ATCC 51449 / 3B1) [Complete proteome] [HAMAP]
Taxonomic identifier235279 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length389 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 – 389389Bifunctional enzyme IspD/IspF HAMAP MF_01520
PRO_0000075668

Regions

Region1 – 2232232-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
Region224 – 3891662-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520

Sites

Metal binding2301Divalent metal cation By similarity
Metal binding2321Divalent metal cation By similarity
Metal binding2641Divalent metal cation By similarity
Site181Transition state stabilizer By similarity
Site311Transition state stabilizer By similarity
Site1491Positions MEP for the nucleophilic attack By similarity
Site2021Positions MEP for the nucleophilic attack By similarity
Site2561Transition state stabilizer By similarity
Site3551Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VFU3 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: ED1973A31627484C

FASTA38943,300
        10         20         30         40         50         60 
MVLDNVSLIM MAAGDSTRFC ASNAQTFRCK KQWLRVGEEP LWLVATRNLT HHFSFKQVIL 

        70         80         90        100        110        120 
TASSKDYVYM QNISPYKVVQ GGQTRCQSLR NALKYVDTPL VLVSDVARWD SSDSIIKTML 

       130        140        150        160        170        180 
KALDESVACV VPFVGVADTS FYEGEYLKRE SIKLIQTPQL SRVEDLQEAL KDTSKDFSDE 

       190        200        210        220        230        240 
SSALYALGKK IAFVQGSELM NKLTFSSDLK AHITRLSPPS KRVFIGNGID VHQFEKNKQM 

       250        260        270        280        290        300 
WLGGVEIESP FGFKAHSDGD VVLHALSDAI LGAIGGGDIG EWFPDTDETY KNADSKMMLS 

       310        320        330        340        350        360 
EIYTFAQSVG YELYNADISI IAQTPKIAPY KSAMRECIAR ILRVPNAHIN IKATTTEGLG 

       370        380 
FVGREEGVCV EACVSMGFIN WHTYIKDLH

« Hide

References

[1]"The complete genome sequence of the carcinogenic bacterium Helicobacter hepaticus."
Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M., Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R., Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B. expand/collapse author list , Shen Z., Weber J., Frosch M., Fox J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003) [PubMed: 12810954] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51449 / 3B1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017125 Genomic DNA. Translation: AAP78179.1.
RefSeqNP_861113.1. NC_004917.1.

3D structure databases

ProteinModelPortalQ7VFU3.
SMRQ7VFU3. Positions 224-376.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1492129.
GenomeReviewsGene locus HH_1582 in contig AE017125_GR.
KEGGhhe:HH1582.
NMPDRfig|235279.1.peg.1582.
PATRIC20590610. VBIHelHep90276_1564.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG672839.
OMAGGDIGEW.
ProtClustDBPRK09382.

Enzyme and pathway databases

BioCycHHEP235279:HH_1582-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.
TIGRFAMsTIGR00151. IspF. 1 hit.
PROSITEPS01295. ISPD. 1 hit.
PS01350. ISPF. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameISPDF_HELHP
AccessionPrimary (citable) accession number: Q7VFU3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: October 1, 2003
Last modified: January 25, 2012
This is version 52 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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