Q7A0R5 (MTNN_STAAW) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 49.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·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 |
| ||||
| Organism | Staphylococcus aureus (strain MW2) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 196620 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 228 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 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 |
| 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 |
| 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 – 228 | 228 | 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase HAMAP MF_01684 | PRO_0000359370 | |||||
Regions | |||||||||
| Region | 172 – 173 | 2 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 11 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 77 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 151 | 1 | Substrate; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Binding site | 196 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "Genome and virulence determinants of high virulence community-acquired MRSA." Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K. Lancet 359:1819-1827(2002) [PubMed: 12044378] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MW2. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000033 Genomic DNA. Translation: BAB95415.1. |
| RefSeq | NP_646367.1. NC_003923.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1JYS based on UniProtKB P0AF12. |
| ProteinModelPortal | Q7A0R5. |
| SMR | Q7A0R5. Positions 2-227. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q7A0R5. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBSTAT00000027025; EBSTAP00000026064; EBSTAG00000027024. |
| GeneID | 1003662. |
| GenomeReviews | Gene locus MW1550 in contig BA000033_GR. |
| KEGG | sam:MW1550. |
| PATRIC | 19569712. VBIStaAur44266_1617. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0775. |
| GeneTree | EBGT00050000025335. |
| HOGENOM | HBG367723. |
| OMA | LEHFPTM. |
| PhylomeDB | Q7A0R5. |
| ProtClustDB | CLSK885455. |
Enzyme and pathway databases | |
| BioCyc | SAUR196620:MW1550-MONOMER. |
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_STAAW | ||||||||
| Accession | Primary (citable) accession number: Q7A0R5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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