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A7GZI1 (ISPDF_CAMC5) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. 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:Ccur92_13190
ORF Names:CCV52592_0202
OrganismCampylobacter curvus (strain 525.92) [Complete proteome] [HAMAP]
Taxonomic identifier360105 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length371 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 – 371371Bifunctional enzyme IspD/IspF HAMAP MF_01520
PRO_0000315551

Regions

Region1 – 2122122-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
Region213 – 3711592-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520

Sites

Metal binding2181Divalent metal cation By similarity
Metal binding2201Divalent metal cation By similarity
Metal binding2521Divalent metal cation By similarity
Site161Transition state stabilizer By similarity
Site231Transition state stabilizer By similarity
Site1391Positions MEP for the nucleophilic attack By similarity
Site1911Positions MEP for the nucleophilic attack By similarity
Site2441Transition state stabilizer By similarity
Site3431Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
A7GZI1 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 19539BC456B583E4

FASTA37140,960
        10         20         30         40         50         60 
MLDISLIMLG AGNSSRFELP VKKQWLRIGS DPLWLAATKN LSEFYTFKDI IVVSKECEYM 

        70         80         90        100        110        120 
ARFAPHYKFV TGGDTRQQSL KNALNLVSSQ FVLVSDIARP CITHELFSKI IEGSKQANCV 

       130        140        150        160        170        180 
VPALKIADTA YFGDEVIDRD KIKLIQTPQL SKTNLLKQAL ETDTLYTDDS SAMRAVGASV 

       190        200        210        220        230        240 
WHVLGDERAH KITTKSDLAK IPCLIPPSNE HFTGIGFDAH EFERGRELWL CGEKIEYEFG 

       250        260        270        280        290        300 
LKAHSDGDVA LHALTDAILG AAGLGDIGEL FPDTDAEFKG ISSLLLLQEA YKKVQSVGFE 

       310        320        330        340        350        360 
LVNADITIMA ERPKISKFKR KMEANIAGAL NLAPNRINVK ATTTEKLGFV GRGEGIAVIA 

       370 
SANLKYYDWT K 

« Hide

References

[1]"Genome sequence of Campylobacter curvus 525.92 isolated from human feces."
Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Lastovica A.J., Nelson K.E.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 525.92.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000767 Genomic DNA. Translation: EAU01256.1.
RefSeqYP_001408623.1. NC_009715.1.

3D structure databases

ProteinModelPortalA7GZI1.
SMRA7GZI1. Positions 3-371.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7GZI1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5407441.
GenomeReviewsGene locus Ccur92_13190 in contig CP000767_GR.
KEGGccv:CCV52592_0202.
PATRIC20033200. VBICamCur47627_1392.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1211.
HOGENOMHBG672839.
OMAIVLIHDA.
ProtClustDBPRK09382.

Enzyme and pathway databases

BioCycCCUR360105:CCV52592_0202-MONOMER.

Family and domain databases

HAMAPMF_01520. IspDF.
[Tree]
InterProIPR023423. IpsF_dom.
IPR001228. ISPD_synthase.
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. False negative.
PS01350. ISPF. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameISPDF_CAMC5
AccessionPrimary (citable) accession number: A7GZI1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 11, 2007
Last modified: January 25, 2012
This is version 33 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