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Q9A7I5 (ISPDF_CAUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 70. 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:CC_1738
OrganismCaulobacter crescentus (Caulobacter vibrioides)
Taxonomic identifier155892 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Caulobacterales › Caulobacteraceae › Caulobacter

Protein attributes

Sequence length382 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 – 382382Bifunctional enzyme IspD/IspF HAMAP MF_01520
PRO_0000075664

Regions

Region1 – 2252252-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
Region226 – 3821572-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520

Sites

Metal binding2321Divalent metal cation By similarity
Metal binding2341Divalent metal cation By similarity
Metal binding2661Divalent metal cation By similarity
Site151Transition state stabilizer By similarity
Site221Transition state stabilizer By similarity
Site1511Positions MEP for the nucleophilic attack By similarity
Site2051Positions MEP for the nucleophilic attack By similarity
Site2581Transition state stabilizer By similarity
Site3571Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9A7I5 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: E2E07773856A317C

FASTA38240,049
        10         20         30         40         50         60 
MTFSVVIVAA GSGTRAGPGQ AKQWRVLAGR PVLRWSVEAF LAAGAAEVVV VTTADGEAFL 

        70         80         90        100        110        120 
PRMLEGLQGW RSTLGGATRA LSVQAGLAAL SERPGAEPVM IHDAARPFVS RNVILALLGA 

       130        140        150        160        170        180 
LSDADLALPA LAVADTLKRQ PTGEAAQTVS REHLWRAQTP QAARRDTLIA AYAAWTHGEP 

       190        200        210        220        230        240 
TDDAQVVEAA GGRIALTAGD PLLTKLTYPE DFAMAEHLAG VARVTRVGQG FDAHRWGPGE 

       250        260        270        280        290        300 
EVWLCGVAIK HDETLVGHSD ADAGLHALTD AILGAIGEGD IGDHFPPTDP KWKGAASDQF 

       310        320        330        340        350        360 
LKHAVDLVTA KGGALVNVDV TLICERPKIK PHRQAMRERL AEILSIPVDR VSVKATTTEK 

       370        380 
MGFTGRGEGL AASAVVAVET PA

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE005673 Genomic DNA. Translation: AAK23714.1.
PIRF87464.
RefSeqNP_420546.1. NC_002696.2.

3D structure databases

ProteinModelPortalQ9A7I5.
SMRQ9A7I5. Positions 225-379.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID942098.
GenomeReviewsGene locus CC_1738 in contig AE005673_GR.
KEGGccr:CC_1738.
NMPDRfig|190650.1.peg.1726.
PATRIC21300492. VBICauCre124313_1762.
TIGRCC_1738.

Phylogenomic databases

HOGENOMHBG672839.
OMAIVLIHDA.
ProtClustDBPRK09382.

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_CAUCR
AccessionPrimary (citable) accession number: Q9A7I5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: June 1, 2001
Last modified: January 25, 2012
This is version 70 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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