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Reviewed, UniProtKB/Swiss-Prot Q9R4A1 (MTNN_KLEPN)

Last modified September 22, 2009. Version 26. 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:
    5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
      Short name=MTA/SAH nucleosidase
      Short name=MTAN
    EC=3.2.2.9
Alternative name(s):
    5'-methylthioadenosine nucleosidase
      Short name=MTA nucleosidase
    S-adenosylhomocysteine nucleosidase
      Short name=SAH nucleosidase
      Short name=AdoHcy nucleosidase
      Short name=SRH nucleosidase
Gene names
Name: mtnN
OrganismKlebsiella pneumoniae
Taxonomic identifier573 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

Protein attributes

Sequence length35 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. HAMAP MF_01684

Catalytic activity

S-adenosyl-L-homocysteine + H2O = S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine. HAMAP MF_01684

S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine. HAMAP MF_01684

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 1/2. HAMAP MF_01684

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the PNP/UDP phosphorylase family. MtnN subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=8.7 µM for 5'-methylthioadenosine (at pH 7 and 37 degrees Celsius) HAMAP MF_01684

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›35›355'-methylthioadenosine/S-adenosylhomocysteine nucleosidase HAMAP MF_01684
PRO_0000359310

Sites

Active site121Proton acceptor By similarity

Experimental info

Non-terminal residue351

Sequences

Sequence LengthMass (Da)Tools
Q9R4A1-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: FB878C0271A01C35

FASTA353,924
        10         20         30 
MKIGIIGAME EEVTLLRDKI ENRQTITIGG SEIYT 

« Hide

References

[1]"Affinity purification of 5-methylthioribose kinase and 5-methylthioadenosine/S-adenosylhomocysteine nucleosidase from Klebsiella pneumoniae."
Cornell K.A., Winter R.W., Tower P.A., Riscoe M.K.
Biochem. J. 317:285-290(1996) [PubMed: 8694776] [Abstract]
Cited for: PROTEIN SEQUENCE, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

3D structure databases

HSSPHSSP built from PDB template 1NC1 based on UniProtKB P24247.
ModBaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MON-1288.

Family and domain databases

HAMAPMF_01684.
[Tree]
ProtoNetSearch...

Entry information

Entry nameMTNN_KLEPN
AccessionPrimary (citable) accession number: Q9R4A1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: May 1, 2000
Last modified: September 22, 2009
This is version 26 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