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P60217 (MTNN_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 51. 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:
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=AdoHcy nucleosidase
Short name=SAH nucleosidase
Short name=SRH nucleosidase
Gene names
Name:mtnN
Synonyms:mtn
Ordered Locus Names:STM0207
OrganismSalmonella typhimurium
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length232 AA.
Sequence statusComplete.
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. 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. HAMAP MF_01684

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2322325'-methylthioadenosine/S-adenosylhomocysteine nucleosidase HAMAP MF_01684
PRO_0000164448

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
P60217 [UniParc].

Last modified January 16, 2004. Version 1.
Checksum: 90E2638E702B9B26

FASTA23224,446
        10         20         30         40         50         60 
MKIGIIGAME EEVTLLRDKI DNRQTITLGG CEIYTGQLNG TEVALLKSGI GKVAAALGAT 

        70         80         90        100        110        120 
LLLEHCKPDV IINTGSAGGL ASTLKVGDIV VSDEARYHDA DVTAFGYEYG QLPGCPAGFK 

       130        140        150        160        170        180 
ADDKLIAAAE SCIRELNLNA VRGLIVSGDA FINGSVGLAK IRHNFPDAVA VEMEATAIAH 

       190        200        210        220        230 
VCHNFNVPFV VVRAISDVAD QQSHLSFDEF LAVAAKQSTL MVETLVQKLA HG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006468 Genomic DNA. Translation: AAL19171.1.
RefSeqNP_459212.1. NC_003197.1.

3D structure databases

ProteinModelPortalP60217.
SMRP60217. Positions 1-232.
ModBaseSearch...

Proteomic databases

PRIDEP60217.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1251725.
GenomeReviewsGene locus STM0207 in contig AE006468_GR.
KEGGstm:STM0207.
PATRIC32378701. VBISalEnt20916_0220.

Phylogenomic databases

HOGENOMHBG367723.
OMAVIGAMEQ.
ProtClustDBPRK05584.

Enzyme and pathway databases

BioCycSTYP99287:STM0207-MONOMER.

Family and domain databases

HAMAPMF_01684. Salvage_tnN.
[Tree]
InterProIPR010049. MTA_SAH_Nsdase.
IPR018017. Nucleoside_phosphorylase.
IPR000845. Nucleoside_phosphorylase_d.
[Graphical view]
KOK01243.
PANTHERPTHR21234. PNP_UDP. 1 hit.
PTHR21234:SF6. PTHR21234:SF6. 1 hit.
PfamPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR01704. MTA/SAH-Nsdase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMTNN_SALTY
AccessionPrimary (citable) accession number: P60217
Secondary accession number(s): Q8XFN5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 16, 2004
Last modified: January 25, 2012
This is version 51 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