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Reviewed, UniProtKB/Swiss-Prot Q3BUE8 (MTNC_XANC5)

Last modified February 9, 2010. Version 36. 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:
    Enolase-phosphatase E1
    EC=3.1.3.77
Alternative name(s):
    2,3-diketo-5-methylthio-1-phosphopentane phosphatase
Gene names
Name: mtnC
Ordered Locus Names: XCV1884
OrganismXanthomonas campestris pv. vesicatoria (strain 85-10) [Complete proteome] [HAMAP]
Taxonomic identifier316273 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length232 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) By similarity. HAMAP MF_01681

Catalytic activity

5-(methylthio)-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate. HAMAP MF_01681

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01681

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6. HAMAP MF_01681

Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 4/6.

Subunit structure

Monomer By similarity. HAMAP MF_01681

Sequence similarities

Belongs to the HAD-like hydrolase superfamily. MasA/mtnC family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 232232Enolase-phosphatase E1 HAMAP MF_01681
PRO_0000357431

Sequences

Sequence LengthMass (Da)Tools
Q3BUE8-1 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: F25A49E69A93420C

FASTA23225,905
        10         20         30         40         50         60 
MTRPQAILTD IEGTTSSISF VKDVLFPYAR RAMPAYVREH GNHPQVRHWL NQVADEIGED 

        70         80         90        100        110        120 
VPDEVLITTL QTWIDEDRKH TALKALQGLI WGDGYKTADF TAHIYADAAI QLKAWHAAGI 

       130        140        150        160        170        180 
PLYVYSSGSV PAQKLFFAHS DAGDLSGLIT DWFDTEVGPK RESASYRRIA ERIGVPGPEI 

       190        200        210        220        230 
LFLSDVIEEL DAAKRAGMRT ALLDRREDYP TPRSADDVGS HQRVESFSQL VL 

« Hide

References

[1]"Insights into genome plasticity and pathogenicity of the plant pathogenic Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete genome sequence."
Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D., Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C., Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H., Niesbach-Kloesgen U. expand/collapse author list , Patschkowski T., Rueckert C., Rupp O., Schneiker S., Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D., Kaiser O.
J. Bacteriol. 187:7254-7266(2005) [PubMed: 16237009] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM039952 Genomic DNA. Translation: CAJ23561.1.
RefSeqYP_363615.1.

3D structure databases

HSSPHSSP built from PDB template 2G80 based on UniProtKB P32626.
SMRQ3BUE8. Positions 3-232.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3BUE8.

Genome annotation databases

GeneID3730668.
GenomeReviewsGene locus XCV1884 in contig AM039952_GR.
KEGGxcv:XCV1884.
NMPDRfig|316273.3.peg.2292.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4229.
HOGENOMHBG294242.
OMATTDLNFI.

Family and domain databases

HAMAPMF_01681. Salvage_MtnC.
[Tree]
InterProIPR010041. Enolase_ppase.
IPR006439. HAD-SF_hydro_IA_v1.
IPR005833. Haloacid_DH/epoxide_hydro.
[Graphical view]
PANTHERPTHR20371. Enolase_ppase. 1 hit.
PRINTSPR00413. HADHALOGNASE.
TIGRFAMsTIGR01691. enolase-ppase. 1 hit.
TIGR01549. HAD-SF-IA-v1. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMTNC_XANC5
AccessionPrimary (citable) accession number: Q3BUE8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: November 22, 2005
Last modified: February 9, 2010
This is version 36 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