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A5EIY9 (ISPDF_BRASB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 32. 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:BBta_4067
OrganismBradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182) [Complete proteome] [HAMAP]
Taxonomic identifier288000 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Bradyrhizobium

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_0000296739

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
A5EIY9 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: FD5015BC3EFA52A5

FASTA39341,631
        10         20         30         40         50         60 
MTISQRTAAI LVAAGRGLRA GTGGPKQYRA IGGRTVIHRA LAAFSEHPDV AVVQPVVNPD 

        70         80         90        100        110        120 
DIDVFNAAVS GLRHEVPAHG GATRQASVLA GLEALVPHRP DIVLIHDAAR PFVTSAVISR 

       130        140        150        160        170        180 
AIQAAGKTGA AIPVVPVTDT IKEVTASGDI IATPERAKLR IAQTPQTFKF EVILEAHRRA 

       190        200        210        220        230        240 
ARDGLTEFTD DAAIAEWAGL TVATFEGDVA NMKLTTPEDF VREEARLAAQ LGDIRTGTGY 

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

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

       370        380        390 
AVKATTSERL GFTGREEGIA ATASATIRLP WSA

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000494 Genomic DNA. Translation: ABQ36133.1.
RefSeqYP_001240039.1. NC_009485.1.

3D structure databases

ProteinModelPortalA5EIY9.
SMRA5EIY9. Positions 234-387.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5EIY9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5153386.
GenomeReviewsGene locus BBta_4067 in contig CP000494_GR.
KEGGbbt:BBta_4067.
PATRIC21208915. VBIBraSp29847_4127.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1211.
HOGENOMHBG672839.
OMAIVLIHDA.
ProtClustDBCLSK911224.

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.
TIGRFAMsTIGR00453. IspD. 1 hit.
TIGR00151. IspF. 1 hit.
PROSITEPS01295. ISPD. 1 hit.
PS01350. ISPF. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameISPDF_BRASB
AccessionPrimary (citable) accession number: A5EIY9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: June 12, 2007
Last modified: January 25, 2012
This is version 32 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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