Reviewed,
UniProtKB/Swiss-Prot P40873 (MSOX_ARTST)
Last modified
November 25, 2008.
Version 68.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
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 names | Recommended name: Monomeric sarcosine oxidase Short name=MSOX EC=1.5.3.1 | ||
| Gene names |
| ||
| Organism | Arthrobacter sp. (strain TE1826) | ||
| Taxonomic identifier | 68999 [NCBI] | ||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter |
Protein attributes
| Sequence length | 389 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the oxidative demethylation of sarcosine. |
| Catalytic activity | Sarcosine + H(2)O + O(2) = glycine + formaldehyde + H(2)O(2). |
| Cofactor | Binds 1 FAD per subunit. |
| Subunit structure | Monomer. |
| Subcellular location | |
| Miscellaneous | Decreases in function by replacement in the G-X-G-X-X-G motif are suppressed by chloride or bromide ion. |
| Sequence similarities | Belongs to the MSOX/MTOX family. MSOX subfamily. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | FAD Flavoprotein |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tetrahydrofolate metabolic processInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: HAMAP |
| Molecular function | sarcosine oxidase activity Inferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed | ||||||
| Chain | 2 – 389 | 388 | Monomeric sarcosine oxidase | PRO_0000213760 | |||||
Regions | |||||||||
| Nucleotide binding | 8 – 38 | 31 | FAD Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 318 | 1 | S-8alpha-FAD cysteine Probable | ||||||
Experimental info | |||||||||
| Mutagenesis | 13 | 1 | G → A: Loss of activity | ||||||
| Mutagenesis | 14 | 1 | A → D or K: Loss of activity | ||||||
| Mutagenesis | 14 | 1 | A → I or V: Decrease in activity | ||||||
| Mutagenesis | 14 | 1 | A → L, W or Y: Weak activity | ||||||
| Mutagenesis | 15 | 1 | G → A: Loss of activity | ||||||
| Mutagenesis | 16 | 1 | S → P: Weak activity. Loss of activity; when associated with G-17 | ||||||
| Mutagenesis | 17 | 1 | M → G: Weak activity. Loss of activity; when associated with P-16 | ||||||
| Mutagenesis | 18 | 1 | G → A: Weak activity | ||||||
| Mutagenesis | 36 | 1 | D → A: Loss of activity | ||||||
| Mutagenesis | 36 | 1 | D → E: Almost no change in activity | ||||||
| Mutagenesis | 36 | 1 | D → N: 100-fold decrease in activity | ||||||
| Mutagenesis | 265 | 1 | C → A or D: Decrease in activity. Stabilizes soxA against chemicals and metal ions | ||||||
| Mutagenesis | 265 | 1 | C → R or S: Almost no change in activity. Stabilizes soxA against chemicals and metal ions | ||||||
| Mutagenesis | 318 | 1 | C → S: Weak activity | ||||||
| Sequence conflict | 39 | 1 | H → D in BAA09716 and BAA25926. Ref.2 | ||||||
| Sequence conflict | 316 | 1 | D → A in BAA09716 and BAA25926. Ref.2 | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Cloning and sequencing of the sarcosine oxidase gene from Arthrobacter sp. TE1826." Nishiya Y., Imanaka T. J. Ferment. Bioeng. 75:239-244(1993) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-6. |
| [2] | "Gene cluster for creatinine degradation in Arthrobacter sp. TE1826." Nishiya Y., Toda A., Imanaka T. Mol. Gen. Genet. 257:581-586(1998) [PubMed: 9563845] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "Active site analysis and stabilization of sarcosine oxidase by the substitution of cysteine residues." Nishiya Y., Zuihara S., Imanaka T. Appl. Environ. Microbiol. 61:367-370(1995) [PubMed: 7887617] [Abstract] Cited for: MUTAGENESIS OF CYS-265 AND CYS-318. |
| [4] | "Analysis of interaction between the Arthrobacter sarcosine oxidase and the coenzyme flavin adenine dinucleotide by site-directed mutagenesis." Nishiya Y., Imanaka T. Appl. Environ. Microbiol. 62:2405-2410(1996) [PubMed: 8779579] [Abstract] Cited for: MUTAGENESIS OF GLY-13; ALA-14; GLY-15; SER-16; MET-17; GLY-18 AND ASP-36. |
| [5] | "A mutant sarcosine oxidase in which activity depends on flavin adenine dinucleotide." Nishiya Y. Protein Expr. Purif. 20:95-97(2000) [PubMed: 11035956] [Abstract] Cited for: MUTAGENESIS OF CYS-318. |
Cross-references
Sequence databases | |
|---|---|
| D63413 Genomic DNA. Translation: BAA09716.1. AB007122 Genomic DNA. Translation: BAA25926.1. | |
| PIR | T44248. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1L9F based on UniProtKB P40859. |
| SMR | P40873. Positions 7-385. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MON-11002. |
Family and domain databases | |
| HAMAP | MF_00516. [Tree] |
| InterPro | IPR006076. FAD-dep_OxRdtase. IPR006281. SoxA_mon. [Graphical view] |
| Pfam | PF01266. DAO. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01377. soxA_mon. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | MSOX_ARTST | ||||||||
| Accession | Primary (citable) accession number: P40873 Secondary accession number(s): O66180 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


