Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot B1I0S9 (ISPDF_DESAP)

Last modified November 3, 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: Daud_0186
OrganismDesulforudis audaxviator (strain MP104C) [Complete proteome] [HAMAP]
Taxonomic identifier477974 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeCandidatus Desulforudis

Protein attributes

Sequence length394 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 – 394394Bifunctional enzyme ispD/ispF HAMAP MF_01520
PRO_1000146271

Regions

Region1 – 2302302-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
Region231 – 3941642-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520

Sites

Metal binding2371Divalent metal cation By similarity
Metal binding2391Divalent metal cation By similarity
Metal binding2711Divalent metal cation By similarity
Site161Transition state stabilizer By similarity
Site231Transition state stabilizer By similarity
Site1551Positions MEP for the nucleophilic attack By similarity
Site2111Positions MEP for the nucleophilic attack By similarity
Site2631Transition state stabilizer By similarity
Site3621Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
B1I0S9-1 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 55EB49DD50524718

FASTA39441,482
        10         20         30         40         50         60 
MADTLAIVVA AGRSSRMGEG PKKQYRLLAG RPVLGRTLEV FEHAPAVDGV VLVVAPGEED 

        70         80         90        100        110        120 
WCREEIVTRF GFTKVVAVVP GGEVRRDSVW AGLQALPPCA LVLVHDGVRP FVTARQIAAV 

       130        140        150        160        170        180 
AEAARECGAA TLAVPPKDTV KLGGPPGAPV STLPRENLWL VQTPQAFRFD VLIKAHHLAR 

       190        200        210        220        230        240 
ERGLAATDDT SLAEAAGYDV RMVPGAYTNI KITTPEDLAF AEALLGGGPV LVGFGYDVHR 

       250        260        270        280        290        300 
LVDDRKLILG GVEVPHDRGL LGHSDADVLV HAVMDALLGA AGAGDIGRWF PDDDPTYRGI 

       310        320        330        340        350        360 
SSMDLLVRVA AFLRERGLET SNLDAVVVAE APRLSPFISR MRDNLASVLG VSPAAVNVKA 

       370        380        390 
TTTEGLGFTG SGAGIAAYAV AALRRIVLPG DRVL 

« Hide

References

[1]"Complete sequence of chromosome of Desulforudis audaxviator MP104C."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F., Land M.L., Hauser L., Kyrpides N., Ivanova N.N., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000860 Genomic DNA. Translation: ACA58750.1.
RefSeqYP_001716382.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6027621.
GenomeReviewsGene locus Daud_0186 in contig CP000860_GR.
KEGGdau:Daud_0186.

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_DESAP
AccessionPrimary (citable) accession number: B1I0S9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: November 3, 2009
This is version 16 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