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Q5FQD6 (ISPDF_GLUOX) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. 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:GOX1669
OrganismGluconobacter oxydans (strain 621H) (Gluconobacter suboxydans) [Complete proteome] [HAMAP]
Taxonomic identifier290633 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Gluconobacter

Protein attributes

Sequence length388 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 caution

The sequence AAW61410.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 388388Bifunctional enzyme IspD/IspF HAMAP MF_01520
PRO_0000075667

Regions

Region1 – 2272272-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
Region228 – 3881612-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520

Sites

Metal binding2341Divalent metal cation By similarity
Metal binding2361Divalent metal cation By similarity
Metal binding2681Divalent metal cation By similarity
Site151Transition state stabilizer By similarity
Site281Transition state stabilizer By similarity
Site1541Positions MEP for the nucleophilic attack By similarity
Site2071Positions MEP for the nucleophilic attack By similarity
Site2601Transition state stabilizer By similarity
Site3591Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5FQD6 [UniParc].

Last modified April 12, 2005. Version 2.
Checksum: B17DEBBD569D502B

FASTA38841,815
        10         20         30         40         50         60 
MRIAALLLAA GRGRRFDASS QSGENSSKQF RMLRGKPVIR RAAEALLPHV DVLLPVGDDP 

        70         80         90        100        110        120 
LLADSLEGLD ILPPVSGGAE RHDSVRNGLE ALAKLPEPPD LVLVHDGARP CVPAEVVQNV 

       130        140        150        160        170        180 
INALKTHEGV IPAVAVIDTI KKAKDGIIVD TVPRDGLWRA QTPQGFRFGT LLELHRTHRD 

       190        200        210        220        230        240 
ARTDDAALLE QAGHPVAIVE GSEDNIKLTV AEDLMRLEGV IDRNLLPRVG LGYDVHAFEE 

       250        260        270        280        290        300 
GRKLILCGIE VPHTKGLAGH SDADVGIHTL CDAIYGALAE GDIGRHFPPS DNKWKDMDSA 

       310        320        330        340        350        360 
RFLVHAGERI RERGGFLVNA DVTLICERPK IGPHAEAMRN RLADLLKVSV SRISVKATTS 

       370        380 
ERLGFTGREE GIAATATVSI MVPDNGEA

« Hide

References

[1]"Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans."
Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., Ehrenreich A., Gottschalk G., Deppenmeier U.
Nat. Biotechnol. 23:195-200(2005) [PubMed: 15665824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 621H.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000009 Genomic DNA. Translation: AAW61410.1. Different initiation.
RefSeqYP_192066.1. NC_006677.1.

3D structure databases

ProteinModelPortalQ5FQD6.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3249409.
GenomeReviewsGene locus GOX1669 in contig CP000009_GR.
KEGGgox:GOX1669.
NMPDRfig|290633.1.peg.1611.
PATRIC32611204. VBIGluOxy81109_1943.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG672839.
ProtClustDBCLSK936440.

Enzyme and pathway databases

BioCycGOXY290633:GOX1669-MONOMER.

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_GLUOX
AccessionPrimary (citable) accession number: Q5FQD6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: April 12, 2005
Last modified: January 25, 2012
This is version 47 of the entry and version 2 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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