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Reviewed, UniProtKB/Swiss-Prot B4EUF0 (MTNN_PROMH)

Last modified November 3, 2009. Version 9. 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
Ordered Locus Names: PMI0214
OrganismProteus mirabilis (strain HI4320) [Complete proteome] [HAMAP]
Taxonomic identifier529507 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

Protein attributes

Sequence length235 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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 By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2352355'-methylthioadenosine/S-adenosylhomocysteine nucleosidase HAMAP MF_01684
PRO_0000359323

Regions

Region173 – 1742Substrate binding By similarity

Sites

Active site121Proton acceptor By similarity
Binding site781Substrate; via amide nitrogen By similarity
Binding site1521Substrate; via amide nitrogen and carbonyl oxygen By similarity
Binding site1971Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B4EUF0-1 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: E184214ECD844845

FASTA23525,208
        10         20         30         40         50         60 
MRVGVIGAME QEVKLLREQI ENCEIVSRGG CEIYTGKING VDVALLKSGI GKVAAAIGTT 

        70         80         90        100        110        120 
LLLEHFRPDV VINTGSAGGL DAKLNVGDIV VSTEVRYHDA DVTAFGYEPG QMAQCPPAFI 

       130        140        150        160        170        180 
ADPKLVNIAQ ECIGSLKLNA VRGLICSGDA FINGAEPLAR IRRTFPEVVA VEMESTAIGH 

       190        200        210        220        230 
VCHQFDTPFV VVRAISDVAD KESHLSFDEF LSVAAQQSSL MVTTMLDKLK TETQF 

« Hide

References

[1]"Complete genome sequence of uropathogenic Proteus mirabilis, a master of both adherence and motility."
Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S., Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T., Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Walker D., Whithead S. expand/collapse author list , Thomson N.R., Rather P.N., Parkhill J., Mobley H.L.T.
J. Bacteriol. 190:4027-4037(2008) [PubMed: 18375554] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AM942759 Genomic DNA. Translation: CAR40612.1.
RefSeqYP_002149995.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6802382.
GenomeReviewsGene locus PMI0214 in contig AM942759_GR.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAAQVCHQF.

Family and domain databases

HAMAPMF_01684.
[Tree]
InterProIPR010049. MTA_SAH_Nsdase.
IPR000845. Nucleoside_phosphorylase.
IPR018017. Nucleoside_phosphorylase_1.
[Graphical view]
PANTHERPTHR21234. PNP_UDP. 1 hit.
PfamPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR01704. MTA/SAH-Nsdase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMTNN_PROMH
AccessionPrimary (citable) accession number: B4EUF0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: September 23, 2008
Last modified: November 3, 2009
This is version 9 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