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Q3SSN8 (ISPDF_NITWN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. 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:Nwi_1442
OrganismNitrobacter winogradskyi (strain Nb-255 / ATCC 25391) [Complete proteome] [HAMAP]
Taxonomic identifier323098 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeNitrobacter

Protein attributes

Sequence length398 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 – 398398Bifunctional enzyme IspD/IspF HAMAP MF_01520
PRO_0000296750

Regions

Region1 – 2342342-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
Region235 – 3981642-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
Q3SSN8 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 2A51DA2EB5BC0930

FASTA39842,115
        10         20         30         40         50         60 
MPSSKRTAAI IVAAGRGLRA GAGGPKQYRT IGGRTVISRA MEAFCQHPDV FAVQPVLNPD 

        70         80         90        100        110        120 
DLSMFNQAAA QFRYRPPANG GATRQASVRA GLEALAADAP DIVLIHDAAR PFVTPALITR 

       130        140        150        160        170        180 
AIDAADKAGA AVPAIAVTDT IKQVDESGAV NATPDRAKLR IAQTPQAFHF DMILDAHRRA 

       190        200        210        220        230        240 
AREGRDDFTD DAALAEWVGL TVATFEGDAA NMKLTTPEDF VREEARLAAA LGDIRTGTGY 

       250        260        270        280        290        300 
DVHAFGEGDH LMLCGVKVPH NCGFLAHSDG DVGLHALVDA ILGALADGDI GSHFPPSDPQ 

       310        320        330        340        350        360 
WKGAASDKFL KYAVDRVTAR GGRVANLEVT MICQQPKIGP LRDQMRARIA DITGVAISRI 

       370        380        390 
AVKATTSERL GFTGREEGIA ATASATIRLP WNDKGRDT 

« Hide

References

[1]"Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium Nitrobacter winogradskyi Nb-255."
Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., Land M.L., Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J., Hickey W.J.
Appl. Environ. Microbiol. 72:2050-2063(2006) [PubMed: 16517654] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Nb-255 / ATCC 25391.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000115 Genomic DNA. Translation: ABA04703.1.
RefSeqYP_318055.1. NC_007406.1.

3D structure databases

HSSPHSSP built from PDB template 1H47 based on UniProtKB P62617.
ProteinModelPortalQ3SSN8.
SMRQ3SSN8. Positions 234-387.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3SSN8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3677184.
GenomeReviewsGene locus Nwi_1442 in contig CP000115_GR.
KEGGnwi:Nwi_1442.
NMPDRfig|323098.3.peg.1517.
PATRIC22699564. VBINitWin102302_1613.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1211.
HOGENOMHBG672839.
OMAIVLIHDA.
PhylomeDBQ3SSN8.
ProtClustDBCLSK911224.

Enzyme and pathway databases

BioCycNWIN323098:NWI_1442-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_NITWN
AccessionPrimary (citable) accession number: Q3SSN8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: October 11, 2005
Last modified: January 25, 2012
This is version 46 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