O32028 (MTNN_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 79.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended 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 |
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| Organism | Bacillus subtilis | ||||||
| Taxonomic identifier | 1423 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 231 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred 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. Ref.2 |
| 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 |
| Sequence similarities | Belongs to the PNP/UDP phosphorylase family. MtnN subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Methionine biosynthesis |
| Molecular function | Hydrolase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | L-methionine salvage from methylthioadenosine Inferred from electronic annotation. Source: InterPro nucleoside catabolic processInferred from electronic annotation. Source: InterPro |
| Molecular function | adenosylhomocysteine nucleosidase activity Inferred from electronic annotation. Source: EC methylthioadenosine nucleosidase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 231 | 231 | 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase HAMAP MF_01684 | PRO_0000164435 | |||||
Regions | |||||||||
| Region | 174 – 175 | 2 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 12 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 78 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 198 | 1 | Substrate By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.  Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [2] | "Identification of yrrU as the methylthioadenosine nucleosidase gene in Bacillus subtilis." Sekowska A., Danchin A. DNA Res. 6:255-264(1999) [PubMed: 10574451] [Abstract] Cited for: FUNCTION. |
| [3] | "The methionine salvage pathway in Bacillus subtilis." Sekowska A., Danchin A. BMC Microbiol. 2:8-8(2002) [PubMed: 12022921] [Abstract] Cited for: REVIEW. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AL009126 Genomic DNA. Translation: CAB14669.1. |
| PIR | D69980. |
| RefSeq | NP_390605.1. NC_000964.3. |
3D structure databases | |
| ProteinModelPortal | O32028. |
| SMR | O32028. Positions 1-230. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000002409; EBBACP00000002409; EBBACG00000002404. |
| GeneID | 938153. |
| GenomeReviews | Gene locus BSU27270 in contig AL009126_GR. |
| KEGG | bsu:BSU27270. |
| NMPDR | fig|224308.1.peg.2730. |
| PATRIC | 18977310. VBIBacSub10457_2844. |
Organism-specific databases | |
| GenoList | BSU27270. [Micado] |
Phylogenomic databases | |
| GeneTree | EBGT00050000000478. |
| HOGENOM | HBG367723. |
| OMA | VIGAMEQ. |
| PhylomeDB | O32028. |
| ProtClustDB | PRK05584. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU27270-MONOMER. MetaCyc:MONOMER-1290. |
Family and domain databases | |
| HAMAP | MF_01684. Salvage_tnN. [Tree] |
| InterPro | IPR010049. MTA_SAH_Nsdase. IPR018017. Nucleoside_phosphorylase. IPR000845. Nucleoside_phosphorylase_d. [Graphical view] |
| KO | K01243. |
| PANTHER | PTHR21234. PNP_UDP. 1 hit. PTHR21234:SF6. PTHR21234:SF6. 1 hit. |
| Pfam | PF01048. PNP_UDP_1. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01704. MTA/SAH-Nsdase. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | MTNN_BACSU | ||||||||
| Accession | Primary (citable) accession number: O32028 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |