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Reviewed, UniProtKB/Swiss-Prot A7HXV6 (ISPDF_PARL1)

Last modified November 3, 2009. Version 15. 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: Plav_3132
OrganismParvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966) [Complete proteome] [HAMAP]
Taxonomic identifier402881 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeParvibaculum

Protein attributes

Sequence length382 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 – 382382Bifunctional enzyme ispD/ispF HAMAP MF_01520
PRO_0000315555

Regions

Region1 – 2262262-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
Region227 – 3821562-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520

Sites

Metal binding2331Divalent metal cation By similarity
Metal binding2351Divalent metal cation By similarity
Metal binding2671Divalent metal cation By similarity
Site151Transition state stabilizer By similarity
Site221Transition state stabilizer By similarity
Site1521Positions MEP for the nucleophilic attack By similarity
Site2061Positions MEP for the nucleophilic attack By similarity
Site2591Transition state stabilizer By similarity
Site3581Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
A7HXV6-1 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: CFAA20EE65BF6F9D

FASTA38239,631
        10         20         30         40         50         60 
MKVAALIVAA GRGSRAGPGA PKQYRLLAGQ PVLRRTLAAF ANHPEIMTVL TVIHPEDASA 

        70         80         90        100        110        120 
FEAASGGLPK LLEPVFGGST RQDSVRAGLE ALNADAPDLV LIHDGARPLI SAPVISACIA 

       130        140        150        160        170        180 
ALSTHEGAQA GLSLTDTIRR TDKGMAAETV ARDTLWRAQT PQAFRFNAIL DAHRQASGGE 

       190        200        210        220        230        240 
HTDDVSVALA AGVKVAMVEG DQDNIKITSA ADIQQAERIL MRSGETRTGL GYDVHRFGPG 

       250        260        270        280        290        300 
DYVWLCGVKV PHDAGLVGHS DADAGLHAIT DAVLGAIGAG DIGRHFPPSD PKWKGAPSEI 

       310        320        330        340        350        360 
FLAHAAKLAT EAGARVSNVD VTLICELPKI GPHADAMRAR IADILGIEKG RVSVKATTTE 

       370        380 
GLGFTGRGEG LAAQAIVTLI IG 

« Hide

References

[1]"Complete genome sequence and annotation of Parvibaculum lavamentivorans DS-1."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000774 Genomic DNA. Translation: ABS64739.1.
RefSeqYP_001414396.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA7HXV6.

Genome annotation databases

GeneID5453865.
GenomeReviewsGene locus Plav_3132 in contig CP000774_GR.
KEGGpla:Plav_3132.

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_PARL1
AccessionPrimary (citable) accession number: A7HXV6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 11, 2007
Last modified: November 3, 2009
This is version 15 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