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Q2W4Q8 (ISPDF_MAGSA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. 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:amb2363
OrganismMagnetospirillum magneticum (strain AMB-1 / ATCC 700264) [Complete proteome] [HAMAP]
Taxonomic identifier342108 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Rhodospirillaceae › Magnetospirillum

Protein attributes

Sequence length384 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 – 384384Bifunctional enzyme IspD/IspF HAMAP MF_01520
PRO_0000292854

Regions

Region1 – 2262262-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
Region227 – 3841582-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520

Sites

Metal binding2331Divalent metal cation By similarity
Metal binding2351Divalent metal cation By similarity
Metal binding2681Divalent metal cation By similarity
Site161Transition state stabilizer By similarity
Site231Transition state stabilizer By similarity
Site1521Positions MEP for the nucleophilic attack By similarity
Site2061Positions MEP for the nucleophilic attack By similarity
Site2601Transition state stabilizer By similarity
Site3591Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2W4Q8 [UniParc].

Last modified January 10, 2006. Version 1.
Checksum: 20AF224F07BB2340

FASTA38440,554
        10         20         30         40         50         60 
MAKTVVLVVA AGRGRRFGGD LPKQYHDLAG RMVLRHTLAA FATNPEIGAV RAVIHPDDRQ 

        70         80         90        100        110        120 
LYDMAAAGLN LLEPVHGGAT RQDSVRLGLD SLKDLNPDKV LIHDGARPFI DHGTIGRVIR 

       130        140        150        160        170        180 
ALDRHPGALP VVPVADTLKR GQDGFVADTV DRANLFRAQT PQGFRYAEIV AAHHAVIGNE 

       190        200        210        220        230        240 
LTDDAAVAEK AGLAVELVNG AEDNVKITTG ADLERARCLF DGPGEVRSAS GYDVHRFDPA 

       250        260        270        280        290        300 
KDACWLCGVP VPHEAGLLGH SDADVGLHAL TDAVLGAISA GDIGHHFPPT DARWKGAASD 

       310        320        330        340        350        360 
QFLAHAGSLV TAKGGRIVNV DVTIICERPK VGPHRAAMAA RVAEILGISQ DRVSVKATTT 

       370        380 
EGLGFTGRKE GIAAQAMASV WLPR

« Hide

References

[1]"Complete genome sequence of the facultative anaerobic magnetotactic bacterium Magnetospirillum sp. strain AMB-1."
Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.
DNA Res. 12:157-166(2005) [PubMed: 16303747] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AMB-1 / ATCC 700264.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP007255 Genomic DNA. Translation: BAE51167.1.
RefSeqYP_421726.1. NC_007626.1.

3D structure databases

HSSPHSSP built from PDB template 1H47 based on UniProtKB P62617.
ProteinModelPortalQ2W4Q8.
SMRQ2W4Q8. Positions 225-381.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2W4Q8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3803940.
GenomeReviewsGene locus amb2363 in contig AP007255_GR.
KEGGmag:amb2363.
NMPDRfig|342108.5.peg.2083.
PATRIC22438984. VBIMagMag129836_2333.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1211.
HOGENOMHBG672839.
OMAIVLIHDA.
PhylomeDBQ2W4Q8.
ProtClustDBCLSK943350.

Enzyme and pathway databases

BioCycMMAG342108:AMB2363-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_MAGSA
AccessionPrimary (citable) accession number: Q2W4Q8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: January 10, 2006
Last modified: January 25, 2012
This is version 44 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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