[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-6. Nishiya Y., Imanaka T.; "Cloning and sequencing of the sarcosine oxidase gene from Arthrobacter sp. TE1826."; J. Ferment. Bioeng. 75:239-244(1993).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/s004380050685; PubMed=9563845 [NCBI, ExPASy, EBI, Israel, Japan] Nishiya Y., Toda A., Imanaka T.; "Gene cluster for creatinine degradation in Arthrobacter sp. TE1826."; Mol. Gen. Genet. 257:581-586(1998).
[3]	MUTAGENESIS OF CYS-265 AND CYS-318. PubMed=7887617 [NCBI, ExPASy, EBI, Israel, Japan] Nishiya Y., Zuihara S., Imanaka T.; "Active site analysis and stabilization of sarcosine oxidase by the substitution of cysteine residues."; Appl. Environ. Microbiol. 61:367-370(1995).
[4]	MUTAGENESIS OF GLY-13; ALA-14; GLY-15; SER-16; MET-17; GLY-18 AND ASP-36. PubMed=8779579 [NCBI, ExPASy, EBI, Israel, Japan] Nishiya Y., Imanaka T.; "Analysis of interaction between the Arthrobacter sarcosine oxidase and the coenzyme flavin adenine dinucleotide by site-directed mutagenesis."; Appl. Environ. Microbiol. 62:2405-2410(1996).
[5]	MUTAGENESIS OF CYS-318. DOI=10.1006/prep.2000.1299; PubMed=11035956 [NCBI, ExPASy, EBI, Israel, Japan] Nishiya Y.; "A mutant sarcosine oxidase in which activity depends on flavin adenine dinucleotide."; Protein Expr. Purif. 20:95-97(2000).

Comments

FUNCTION: Catalyzes the oxidative demethylation of sarcosine.
CATALYTIC ACTIVITY: Sarcosine + H₂O + O₂ = glycine + formaldehyde + H₂O₂.
COFACTOR: Binds 1 FAD per subunit.
SUBUNIT: Monomer.
SUBCELLULAR LOCATION: Cytoplasm.
MISCELLANEOUS: Decreases in function by replacement in the G-X-G-X-X-G motif are suppressed by chloride or bromide ion.
SIMILARITY: Belongs to the MSOX/MTOX family. MSOX subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D63413; BAA09716.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB007122; BAA25926.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T44248; T44248.

3D structure databases

HSSP

P40859; 1L9F. [HSSP ENTRY / PDB]

SMR

P40873; 7-385.

ModBase

P40873.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-11002; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0008115;	Molecular function: sarcosine oxidase activity (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00516; -; 1.
PBIL [Tree]

InterPro

IPR006076; FAD-dep_OxRdtase.
IPR006281; SoxA_mon.
Graphical view of domain structure.

Pfam

PF01266; DAO; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01377; soxA_mon; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 389`	`388`	`Monomeric sarcosine oxidase.`	`PRO_0000213760`
`NP_BIND`	`8 38`	`31`	`FAD (Potential).`
`MOD_RES`	`318 318`		`S-8alpha-FAD cysteine (Probable).`
`MUTAGEN`	`13 13`		`G->A: Loss of activity.`
`MUTAGEN`	`14 14`		`A->D,K: Loss of activity.`
`MUTAGEN`	`14 14`		`A->I,V: Decrease in activity.`
`MUTAGEN`	`14 14`		`A->L,W,Y: Weak activity.`
`MUTAGEN`	`15 15`		`G->A: Loss of activity.`
`MUTAGEN`	`16 16`		`S->P: Weak activity. Loss of activity; when associated with G-17.`
`MUTAGEN`	`17 17`		`M->G: Weak activity. Loss of activity; when associated with P-16.`
`MUTAGEN`	`18 18`		`G->A: Weak activity.`
`MUTAGEN`	`36 36`		`D->A: Loss of activity.`
`MUTAGEN`	`36 36`		`D->E: Almost no change in activity.`
`MUTAGEN`	`36 36`		`D->N: 100-fold decrease in activity.`
`MUTAGEN`	`265 265`		`C->A,D: Decrease in activity. Stabilizes soxA against chemicals and metal ions.`
`MUTAGEN`	`265 265`		`C->R,S: Almost no change in activity. Stabilizes soxA against chemicals and metal ions.`
`MUTAGEN`	`318 318`		`C->S: Weak activity.`
`CONFLICT`	`39 39`		`H -> D (in Ref. 2; BAA09716/BAA25926).`
`CONFLICT`	`316 316`		`D -> A (in Ref. 2; BAA09716/BAA25926).`

Sequence information

Length: 389 AA [This is the length of the unprocessed precursor]

Molecular weight: 43294 Da [This is the MW of the unprocessed precursor]

CRC64: 77437C4F12B4AC7F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSIKKDYDVI VVGAGSMGMA AGYYLSKQGV KTLLVDSFHP PHTNGSHHGD TRIIRHAYGE 

        70         80         90        100        110        120 
GREYVPFALR AQELWYELEK ETHHKIFTKT GVLVFGPKGE APFVAETMEA AKEHSLDVDL 

       130        140        150        160        170        180 
LEGSEINKRW PGVTVPENYN AIFEKNSGVL FSENCIRAYR ELAEANGAKV LTYTPVEDFE 

       190        200        210        220        230        240 
IAEDFVKIQT AYGSFTASKL IVSMGAWNSK LLSKLNIEIP LQPYRQVVGF FECDEKKYSN 

       250        260        270        280        290        300 
THGYPAFMVE VPTGIYYGFP SFGGCGLKIG YHTYGQKIDP DTINREFGIY PEDEGNIRKF 

       310        320        330        340        350        360 
LETYMPGATG ELKSGDVCMY TKTPDEHFVI DLHPQFSNVA IAAGFSGHGF KFSSVVGETL 

       370        380 
SQLAVTGKTE HDISIFSINR PALKQKETI

P40873 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools