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Reviewed, UniProtKB/Swiss-Prot A5CTY4 (ISPDF_CLAM3)

Last modified November 3, 2009. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Bifunctional enzyme ispD/ispF
Including the following 2 domains:
    1- Recommended name:
            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- Recommended name:
            2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
                Short name=MECPS
                Short name=MECDP-synthase
              EC=4.6.1.12
Gene names
Name: ispDF
Ordered Locus Names: CMM_2489
OrganismClavibacter michiganensis subsp. michiganensis (strain NCPPB 382) [Complete proteome] [HAMAP]
Taxonomic identifier443906 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrobacteriaceaeClavibacter

Protein attributes

Sequence length410 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

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 – 410410Bifunctional enzyme ispD/ispF HAMAP MF_01520
PRO_0000315552

Regions

Region1 – 2572572-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
Region258 – 4101532-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520

Sites

Metal binding2641Divalent metal cation By similarity
Metal binding2661Divalent metal cation By similarity
Metal binding2981Divalent metal cation By similarity
Site351Transition state stabilizer By similarity
Site421Transition state stabilizer By similarity
Site1771Positions MEP for the nucleophilic attack By similarity
Site2301Positions MEP for the nucleophilic attack By similarity
Site2901Transition state stabilizer By similarity
Site3861Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
A5CTY4-1 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 987E4DA39C126EF3

FASTA41040,906
        10         20         30         40         50         60 
MSHDPVVPSA PATDGGATDG PRLGVVVVAA GSGTRLGAGI PKALVEVGGV TLLARSLSSV 

        70         80         90        100        110        120 
LGLAEEAHVV VVAPDTHLAE TSAVVDAVAG AARGSVAVVV GGATRQGSVR AGLAALVGSV 

       130        140        150        160        170        180 
DTVLVHDAAR ALTPTDLFAA VARAVRAEGA GVVPGLPVTD TVKRVDPAGE CLGTVDRSDL 

       190        200        210        220        230        240 
VGVQTPQGFP RAALDAAYAR AAAEHTDDAA LFQASGGRVR VIPGDALAFK VTTAWDLRRA 

       250        260        270        280        290        300 
EELVARDAGA GSASSRLRSG IGTDVHAVDA SQPLWLAGLH WPGEAGLAGH SDGDAVSHAM 

       310        320        330        340        350        360 
CDALLSAAGL GDIGGIFGTD DPELDGAHGE VFLRRTAELV RDAGYRIVNV AVQVMAVRPK 

       370        380        390        400        410 
LSPRRAEAER ILSAAVGAPV SLAGTTTDGL GFTGRGDGVA AVATALVERL 

« Hide

References

[1]"The genome sequence of the tomato-pathogenic actinomycete Clavibacter michiganensis subsp. michiganensis NCPPB382 reveals a large island involved in pathogenicity."
Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M., Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O., Kirchner O., Krause L., Linke B., McHardy A., Meyer F., Pohle S., Rueckert C. expand/collapse author list , Schneiker S., Zellermann E.-M., Puehler A., Eichenlaub R., Kaiser O., Bartels D.
J. Bacteriol. 190:2138-2149(2008) [PubMed: 18192381] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AM711867 Genomic DNA. Translation: CAN02570.1.
RefSeqYP_001223233.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA5CTY4.

Genome annotation databases

GeneID5174582.
GenomeReviewsGene locus CMM_2489 in contig AM711867_GR.
KEGGcmi:CMM_2489.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAIVLIHDA.

Family and domain databases

HAMAPMF_01520.
[Tree]
InterProIPR001228. ISPD_synthase.
IPR018294. ISPD_synthase_CS.
IPR003526. MECDP_synthase_core.
IPR020555. MECDP_synthase_CS.
[Graphical view]
PfamPF01128. IspD. 1 hit.
PF02542. YgbB. 1 hit.
[Graphical view]
TIGRFAMsTIGR00453. ispD. 1 hit.
TIGR00151. ispF. 1 hit.
PROSITEPS01295. ISPD. 1 hit.
PS01350. ISPF. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameISPDF_CLAM3
AccessionPrimary (citable) accession number: A5CTY4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 12, 2007
Last modified: November 3, 2009
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents