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Reviewed, UniProtKB/Swiss-Prot A1B890 (ISPDF_PARDP)

Last modified October 13, 2009. Version 16. 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: Pden_3667
OrganismParacoccus denitrificans (strain Pd 1222) [Complete proteome] [HAMAP]
Taxonomic identifier318586 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Protein attributes

Sequence length380 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 – 380380Bifunctional enzyme ispD/ispF HAMAP MF_01520
PRO_0000292858

Regions

Region1 – 2242242-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
Region225 – 3801562-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520

Sites

Metal binding2311Divalent metal cation By similarity
Metal binding2331Divalent metal cation By similarity
Metal binding2651Divalent metal cation By similarity
Site191Transition state stabilizer By similarity
Site261Transition state stabilizer By similarity
Site1511Positions MEP for the nucleophilic attack By similarity
Site2041Positions MEP for the nucleophilic attack By similarity
Site2571Transition state stabilizer By similarity
Site3561Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
A1B890-1 [UniParc].

Last modified June 26, 2007. Version 2.
Checksum: FF37E37D79F81468

FASTA38039,647
        10         20         30         40         50         60 
MTIPATYAAI ITAAGRGTRA GDGPPKQWRP LAGQSVLERS IAAFAGFPRV VVTLAPEDMA 

        70         80         90        100        110        120 
RGVAELSGPV VLVAGGATRS DSVRAALESL EGSGVTHVLI HDGARPLVSR RVIGGVIEAL 

       130        140        150        160        170        180 
QSGAPAAAPA LPVTDALWRA QDGCVTATAS REGLFRAQTP QGFALDAILA AHRAHPEGAA 

       190        200        210        220        230        240 
DDVELAIRAG LPVTVTPGDE DNLKLTWPGD FARAERILGD AMDIRLGNGF DVHAFTTGDH 

       250        260        270        280        290        300 
VWLCGVKIPH DKALLGHSDA DVGMHALTDA IYGALAQGDI GRHFPPSDPQ WKGAESHIFL 

       310        320        330        340        350        360 
RHAAMLARQM GYEISNADVT LICERPKVGP HAGAMALRLS EIIGVEPDRV SVKATTSERL 

       370        380 
GFTGREEGIA SIATATLVKG 

« Hide

References

[1]"Complete sequence of chromosome 2 of Paracoccus denitrificans PD1222."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000490 Genomic DNA. Translation: ABL71734.1. Different initiation.
RefSeqYP_917430.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA1B890.

Genome annotation databases

GeneID4582219.
GenomeReviewsGene locus Pden_3667 in contig CP000490_GR.
KEGGpde:Pden_3667.

Organism-specific databases

CMRSearch...

Family and domain databases

HAMAPMF_01520.
[Tree]
InterProIPR001228. ISPD_synthase.
IPR018294. ISPD_synthase_CS.
IPR003526. MECDP_synthase_core.
IPR020555. MECDP_synthase_CS.
[Graphical view]
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_PARDP
AccessionPrimary (citable) accession number: A1B890
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: October 13, 2009
This is version 16 of the entry and version 2 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