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Reviewed, UniProtKB/Swiss-Prot Q828K9 (MTNC_STRAW)

Last modified November 3, 2009. Version 43. 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: SAV_6660
OrganismStreptomyces avermitilis [Complete proteome] [HAMAP]
Taxonomic identifier33903 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length239 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 – 239239Enolase-phosphatase E1 HAMAP MF_01681
PRO_0000357416

Sequences

Sequence LengthMass (Da)Tools
Q828K9-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: A9AF07B31915A758

FASTA23925,809
        10         20         30         40         50         60 
MSSVFDIDSV VLDIEGTTSA TGFVVDVLYP YSRSRFGALL TERSGDPEVA RAVAQVRELL 

        70         80         90        100        110        120 
GEPDADAVRV EKALNEWLDD DRKATPLKTL QGLVWSEGFA RGELVSHFYD DVVPALRAWH 

       130        140        150        160        170        180 
AAGVRLHVYS SGSVAAQRAW FRSSPEGDLL PLVEGLYDTE NAGPKQEPES YRTIAAALGT 

       190        200        210        220        230 
GADRILFLSD RPGELDAARA AGWRTVGVRR PGEPYYEQGV GDHAQAGSFG GITIARSTA 

« Hide

References

[1]"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed: 11572948] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.
[2]"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
Nat. Biotechnol. 21:526-531(2003) [PubMed: 12692562] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

Cross-references

Sequence databases

BA000030 Genomic DNA. Translation: BAC74371.1.
RefSeqNP_827836.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1211526.
GenomeReviewsGene locus SAV_6660 in contig BA000030_GR.
KEGGsma:SAV_6660.
NMPDRfig|227882.1.peg.6662.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ828K9.
OMATTDLNFI.

Enzyme and pathway databases

BioCycSAVE227882:SAV6660-MON.

Family and domain databases

HAMAPMF_01681.
[Tree]
InterProIPR005834. Dehalogen-like_hydro.
IPR010041. Enolase_ppase.
[Graphical view]
PANTHERPTHR20371. Enolase_ppase. 1 hit.
PfamPF00702. Hydrolase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01691. enolase-ppase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMTNC_STRAW
AccessionPrimary (citable) accession number: Q828K9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 43 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