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A6V7A6 (MTNC_PSEA7) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 31. 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:
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:PSPA7_3587
OrganismPseudomonas aeruginosa (strain PA7) [Complete proteome] [HAMAP]
Taxonomic identifier381754 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length225 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 – 225225Enolase-phosphatase E1 HAMAP MF_01681
PRO_0000357388

Sequences

Sequence LengthMass (Da)Tools
A6V7A6 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: D01E425795FA3DD9

FASTA22523,983
        10         20         30         40         50         60 
MTIKAILTDI EGTTSAVSFV FEVLFPYAAR HLPDFVREHA GEAEVAAQLD AVRAASGEAD 

        70         80         90        100        110        120 
AGVERVIAIL LQWIAEDRKA TPLKTLQGMV WAQGYRDGQL KGHVYPDAAQ ALREWKARGL 

       130        140        150        160        170        180 
DLYVYSSGSI QAQKLIFGCS EAGDLGPLFS GYFDTTSGPK RESASYARIA GAIGLPAAQI 

       190        200        210        220 
LFLSDVVQEL DAARDAGLRT LGVAREGGSL DGHPTVASFA DIVVE 

« Hide

References

[1]Dodson R.J., Harkins D., Paulsen I.T.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PA7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000744 Genomic DNA. Translation: ABR86072.1.
RefSeqYP_001348941.1. NC_009656.1.

3D structure databases

ProteinModelPortalA6V7A6.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6V7A6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5357751.
GenomeReviewsGene locus PSPA7_3587 in contig CP000744_GR.
KEGGpap:PSPA7_3587.
PATRIC19828822. VBIPseAer80442_3418.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4229.
HOGENOMHBG294242.
OMATTDLNFI.
ProtClustDBCLSK866737.

Family and domain databases

HAMAPMF_01681. Salvage_MtnC.
[Tree]
InterProIPR005834. Dehalogen-like_hydro.
IPR023943. Enolase-phosphatase_E1.
IPR010041. Enolase_ppase.
IPR023214. HAD-like_dom.
IPR005833. Haloacid_DH/epoxide_hydro.
[Graphical view]
Gene3DG3DSA:3.40.50.1000. HAD-like_dom. 1 hit.
KOK09880.
PfamPF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00413. HADHALOGNASE.
SUPFAMSSF56784. HAD-like_dom. 1 hit.
TIGRFAMsTIGR01691. Enolase-ppase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMTNC_PSEA7
AccessionPrimary (citable) accession number: A6V7A6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: August 21, 2007
Last modified: December 14, 2011
This is version 31 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