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Reviewed, UniProtKB/Swiss-Prot Q5H0Y0 (MTNC_XANOR)

Last modified November 3, 2009. Version 33. 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: XOO2137
OrganismXanthomonas oryzae pv. oryzae [Complete proteome] [HAMAP]
Taxonomic identifier64187 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length232 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

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.

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_0000357432

Experimental info

Sequence conflict1981I → M in AAT48366. Ref.1
Sequence conflict2261S → N in AAT48366. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q5H0Y0-1 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 89F69B08F5DDD0E8

FASTA23225,931
        10         20         30         40         50         60 
MTRPQAILTD IEGTTSSISF VKDVLFPYAR RAMPAYVREH GNHPQVRHWL NQVADEIGED 

        70         80         90        100        110        120 
VPDDVLITTL QTWIDEDRKH TALKALQGLI WGDGYKIADF TAHMYADAAL QLQAWHAAGI 

       130        140        150        160        170        180 
PLYVYSSGSV PAQKLFFAHS DAGDLSGLVS DWFDTEVGSK REAASYRRIA ERIGVPASEI 

       190        200        210        220        230 
LFLSDVIEEL DAAKRTGIRT ALLERREDYP TPRSADDVGS HQRVESFSQL VF 

« Hide

References

« Hide 'large scale' references
[1]"Overexpression of the enolase-phosphatase-like gene in vivo reduces the fitness of Xanthomonas oryzae pv. oryzae in rice cultivars."
Zhang Y., Wang J.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the bacterial blight pathogen of rice."
Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S., Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H., Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S., Go S.-J.
Nucleic Acids Res. 33:577-586(2005) [PubMed: 15673718] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KACC10331 / KXO85.

Cross-references

Sequence databases

AY588249 Genomic DNA. Translation: AAT48366.2.
AE013598 Genomic DNA. Translation: AAW75391.1.
RefSeqYP_200776.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3263813.
GenomeReviewsGene locus XOO2137 in contig AE013598_GR.
KEGGxoo:XOO2137.
NMPDRfig|291331.3.peg.2398.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5H0Y0.
OMATTDLNFI.

Enzyme and pathway databases

BioCycXORY291331:XOO2137-MON.

Family and domain databases

HAMAPMF_01681.
[Tree]
InterProIPR005834. Dehalogen-like_hydro.
IPR010041. Enolase_ppase.
IPR006439. HAD-SF_hydro_IA_v1.
IPR006402. HAD-SF_hydro_IA_v3.
IPR005833. Haloacid_DH/epoxide_hydro.
[Graphical view]
PANTHERPTHR20371. Enolase_ppase. 1 hit.
PfamPF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00413. HADHALOGNASE.
TIGRFAMsTIGR01691. enolase-ppase. 1 hit.
TIGR01549. HAD-SF-IA-v1. 1 hit.
TIGR01509. HAD-SF-IA-v3. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMTNC_XANOR
AccessionPrimary (citable) accession number: Q5H0Y0
Secondary accession number(s): Q6GYR5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: March 1, 2005
Last modified: November 3, 2009
This is version 33 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