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Reviewed, UniProtKB/Swiss-Prot A4YUQ7 (ISPDF_BRASO)

Last modified February 9, 2010. Version 18. 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: BRADO3869
OrganismBradyrhizobium sp. (strain ORS278) [Complete proteome] [HAMAP]
Taxonomic identifier114615 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length393 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 – 393393Bifunctional enzyme ispD/ispF HAMAP MF_01520
PRO_0000296740

Regions

Region1 – 2342342-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
Region235 – 3931592-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520

Sites

Metal binding2411Divalent metal cation By similarity
Metal binding2431Divalent metal cation By similarity
Metal binding2751Divalent metal cation By similarity
Site191Transition state stabilizer By similarity
Site261Transition state stabilizer By similarity
Site1561Positions MEP for the nucleophilic attack By similarity
Site2131Positions MEP for the nucleophilic attack By similarity
Site2671Transition state stabilizer By similarity
Site3661Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
A4YUQ7-1 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: E32987984359AE9B

FASTA39341,489
        10         20         30         40         50         60 
MTTSQRTAAI LVAAGRGLRA GAGGPKQYRT IGGRTVIHRA LAAFAEHPEV AVVQPVVNPD 

        70         80         90        100        110        120 
DIDVFNAAVA GLRHEAPARG GATRQASVLA GLEALVPHKP EIVLIHDAAR PFVTPAVISR 

       130        140        150        160        170        180 
AIIAANKTGA AIPVAPVTDT IKEVGASGDI TATPERAKLR IAQTPQTFRF DTILEAHRRA 

       190        200        210        220        230        240 
AREGLTEFTD DAAIAEWAGL TVATFEGDVA NMKLTTPEDF VREEARLAAS LGDIRTGTGY 

       250        260        270        280        290        300 
DVHAFGEGDH VWLCGLRVPH TKGFLAHSDG DVGLHALVDA ILGALADGDI GSHFPPSDMK 

       310        320        330        340        350        360 
WKGASSDQFL KYAIERVAAR GGRVANLEVT MICERPKIGP LRDQMRARIA EISGVDISRI 

       370        380        390 
AVKATTSERL GFTGREEGIA ATASATIRLP WGA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU234118 Genomic DNA. Translation: CAL77633.1.
RefSeqYP_001205858.1.

3D structure databases

SMRA4YUQ7. Positions 6-392.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4YUQ7.

Genome annotation databases

GeneID5117686.
GenomeReviewsGene locus BRADO3869 in contig CU234118_GR.
KEGGbra:BRADO3869.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1211.
HOGENOMHBG672839.
OMAIVLIHDA.

Family and domain databases

HAMAPMF_01520. IspDF.
[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_BRASO
AccessionPrimary (citable) accession number: A4YUQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: May 29, 2007
Last modified: February 9, 2010
This is version 18 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