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Q2G708 (ISPDF_NOVAD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. 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:Saro_1925
OrganismNovosphingobium aromaticivorans (strain DSM 12444) [Complete proteome] [HAMAP]
Taxonomic identifier279238 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Sphingomonadales › Sphingomonadaceae › Novosphingobium

Protein attributes

Sequence length386 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 – 386386Bifunctional enzyme IspD/IspF HAMAP MF_01520
PRO_0000292857

Regions

Region1 – 2302302-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
Region231 – 3861562-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520

Sites

Metal binding2371Divalent metal cation By similarity
Metal binding2391Divalent metal cation By similarity
Metal binding2711Divalent metal cation By similarity
Site241Transition state stabilizer By similarity
Site311Transition state stabilizer By similarity
Site1591Positions MEP for the nucleophilic attack By similarity
Site2141Positions MEP for the nucleophilic attack By similarity
Site2631Transition state stabilizer By similarity
Site3621Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2G708 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 716C422DEB3B7D17

FASTA38640,153
        10         20         30         40         50         60 
MNSVPSLPGQ SVAAVVVAGG KGLRTGGPVP KQFVIWRGKP LLRHCVEALE AAGIAPIVVA 

        70         80         90        100        110        120 
IPAGWDEAAT QALAGISMVR LVHGGATRQE SVKAALEVLE GDAPARVLIH DAARPDLPGS 

       130        140        150        160        170        180 
VIERLLTALD KRTGAIPVLP VVDSMVRGSG DAMGETVARE DLYRVQTPQA FHYPAILAAH 

       190        200        210        220        230        240 
RAWQGEALAG DDAQVAMRAA HEIALVEGDE ALRKVTFASD LEEQSMSVIP RTGMGFDVHR 

       250        260        270        280        290        300 
LVEGEELWLC GVNIPHGKGL SGHSDADVAI HALVDALLGA IAAGDIGDHF PPSDPQWKGA 

       310        320        330        340        350        360 
SSDRFLAHAG TLVTEAGYRI ANVDVTIICE APKIGPHKAA MRETLARILG IDSALVSVKA 

       370        380 
TTTERLGLTG RGEGIAAQAV ATVVSG

« Hide

References

[1]"Complete sequence of Novosphingobium aromaticivorans DSM 12444."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N. expand/collapse author list , Fredrickson J., Balkwill D., Romine M.F., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 12444.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000248 Genomic DNA. Translation: ABD26365.1.
RefSeqYP_497199.1. NC_007794.1.

3D structure databases

ProteinModelPortalQ2G708.
SMRQ2G708. Positions 231-384.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2G708.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3917148.
GenomeReviewsGene locus Saro_1925 in contig CP000248_GR.
KEGGnar:Saro_1925.
NMPDRfig|48935.1.peg.896.
PATRIC22786556. VBINovAro50627_1971.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1211.
HOGENOMHBG672839.
OMAIVLIHDA.
PhylomeDBQ2G708.
ProtClustDBPRK09382.

Enzyme and pathway databases

BioCycNARO279238:SARO_1925-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_NOVAD
AccessionPrimary (citable) accession number: Q2G708
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: March 21, 2006
Last modified: January 25, 2012
This is version 40 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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