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Q3ZUZ9 (MTNC_ENTSA) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 35. 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
OrganismEnterobacter sakazakii
Taxonomic identifier28141 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCronobacter

Protein attributes

Sequence length229 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 – 229229Enolase-phosphatase E1 HAMAP MF_01681
PRO_0000357361

Sequences

Sequence LengthMass (Da)Tools
Q3ZUZ9 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: 19D9AA9251F569B9

FASTA22926,176
        10         20         30         40         50         60 
MIRAIVTDIE GTTTDIRFVH NVLFPYARER LERFIRSGEQ REPVNLLLNE LRGEIHAPAA 

        70         80         90        100        110        120 
SVDQLIETLF KFMDEDRKSP ALKSIQGYIW REGYVNGDFT GHLYPDVVPA LRRWSDQDID 

       130        140        150        160        170        180 
IYIYSSGSVP AQKLLFSHSD EGDVTELLSG FFDTHVGAKR QVSSYRNISM KTGVPVHQML 

       190        200        210        220 
FLSDIREELD AAREAGWKTV QLIRGEPDTQ STHRQVSSFD DIHPEQIPT 

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References

[1]"Molecular characterization of the alpha-glucosidase activity in Enterobacter sakazakii reveals the presence of a putative gene cluster for palatinose metabolism."
Lehner A., Riedel K., Rattei T., Ruepp A., Frishman D., Breeuwer P., Diep B., Eberl L., Stephan R.
Syst. Appl. Microbiol. 29:609-625(2006) [PubMed: 16563686] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 858.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM075208 Genomic DNA. Translation: CAJ27335.1.

3D structure databases

HSSPHSSP built from PDB template 2G80 based on UniProtKB P32626.
ProteinModelPortalQ3ZUZ9.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

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

Entry information

Entry nameMTNC_ENTSA
AccessionPrimary (citable) accession number: Q3ZUZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: September 27, 2005
Last modified: September 21, 2011
This is version 35 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