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Reviewed, UniProtKB/Swiss-Prot O67786 (MTNC_AQUAE)

Last modified November 3, 2009. Version 50. 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: aq_1977
OrganismAquifex aeolicus [Complete proteome] [HAMAP]
Taxonomic identifier63363 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length223 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 – 223223Enolase-phosphatase E1 HAMAP MF_01681
PRO_0000357358

Sequences

Sequence LengthMass (Da)Tools
O67786-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 5BA39504CFD5979F

FASTA22325,794
        10         20         30         40         50         60 
MVKAILLDIE GTIAPLSFVK EVMFPYSKKK LREFLEKNWE KPEIKKIVQE VEKIEGRELS 

        70         80         90        100        110        120 
LEEAVQLFSR WIDEDRKITP LKELQGHIWE EGFKSGELKA PLYEDAYEKI KEWKEKGIPV 

       130        140        150        160        170        180 
YIYSSGSVKA QNLFFGHSVY GDIRNLFSGF FDTKIGSKRE RSSYEKIAKE IGLPPHEILF 

       190        200        210        220 
ISDNPEELKA AKEAGMKVIQ SVREGVEPSG DFEKITSFRE LEI 

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.

Cross-references

Sequence databases

AE000657 Genomic DNA. Translation: AAC07754.1.
PIRF70469.
RefSeqNP_214355.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1193683.
GenomeReviewsGene locus aq_1977 in contig AE000657_GR.
KEGGaae:aq_1977.
NMPDRfig|224324.1.peg.1370.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO67786.
OMATTDLNFI.

Enzyme and pathway databases

BioCycAAEO224324:AQ_1977-MON.

Family and domain databases

HAMAPMF_01681.
[Tree]
InterProIPR005834. Dehalogen-like_hydro.
IPR010041. Enolase_ppase.
IPR006439. HAD-SF_hydro_IA_v1.
[Graphical view]
PANTHERPTHR20371. Enolase_ppase. 1 hit.
PfamPF00702. Hydrolase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01691. enolase-ppase. 1 hit.
TIGR01549. HAD-SF-IA-v1. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMTNC_AQUAE
AccessionPrimary (citable) accession number: O67786
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: August 1, 1998
Last modified: November 3, 2009
This is version 50 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