ID MSOX_ARTST Reviewed; 389 AA. AC P40873; O66180; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 18-JUN-2025, entry version 117. DE RecName: Full=Monomeric sarcosine oxidase; DE Short=MSOX; DE EC=1.5.3.1; GN Name=soxA; OS Arthrobacter sp. (strain TE1826). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales; OC Micrococcaceae; Arthrobacter. OX NCBI_TaxID=68999; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-6. RA Nishiya Y., Imanaka T.; RT "Cloning and sequencing of the sarcosine oxidase gene from Arthrobacter sp. RT TE1826."; RL J. Ferment. Bioeng. 75:239-244(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9563845; DOI=10.1007/s004380050685; RA Nishiya Y., Toda A., Imanaka T.; RT "Gene cluster for creatinine degradation in Arthrobacter sp. TE1826."; RL Mol. Gen. Genet. 257:581-586(1998). RN [3] RP MUTAGENESIS OF CYS-265 AND CYS-318. RX PubMed=7887617; DOI=10.1128/aem.61.1.367-370.1995; RA Nishiya Y., Zuihara S., Imanaka T.; RT "Active site analysis and stabilization of sarcosine oxidase by the RT substitution of cysteine residues."; RL Appl. Environ. Microbiol. 61:367-370(1995). RN [4] RP MUTAGENESIS OF GLY-13; ALA-14; GLY-15; SER-16; MET-17; GLY-18 AND ASP-36. RX PubMed=8779579; DOI=10.1128/aem.62.7.2405-2410.1996; RA Nishiya Y., Imanaka T.; RT "Analysis of interaction between the Arthrobacter sarcosine oxidase and the RT coenzyme flavin adenine dinucleotide by site-directed mutagenesis."; RL Appl. Environ. Microbiol. 62:2405-2410(1996). RN [5] RP MUTAGENESIS OF CYS-318. RX PubMed=11035956; DOI=10.1006/prep.2000.1299; RA Nishiya Y.; RT "A mutant sarcosine oxidase in which activity depends on flavin adenine RT dinucleotide."; RL Protein Expr. Purif. 20:95-97(2000). CC -!- FUNCTION: Catalyzes the oxidative demethylation of sarcosine. CC -!- CATALYTIC ACTIVITY: CC Reaction=sarcosine + O2 + H2O = formaldehyde + glycine + H2O2; CC Xref=Rhea:RHEA:13313, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16842, ChEBI:CHEBI:57305, CC ChEBI:CHEBI:57433; EC=1.5.3.1; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Note=Binds 1 FAD per subunit.; CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- MISCELLANEOUS: Decreases in function by replacement in the G-X-G-X-X-G CC motif are suppressed by chloride or bromide ion. CC -!- SIMILARITY: Belongs to the MSOX/MTOX family. MSOX subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D63413; BAA09716.1; -; Genomic_DNA. DR EMBL; AB007122; BAA25926.1; -; Genomic_DNA. DR PIR; T44248; T44248. DR AlphaFoldDB; P40873; -. DR SMR; P40873; -. DR BioCyc; MetaCyc:MONOMER-11002; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0008115; F:sarcosine oxidase activity; IEA:UniProtKB-UniRule. DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1. DR HAMAP; MF_00516; MSOX; 1. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR045170; MTOX. DR InterPro; IPR006281; SoxA_mon. DR NCBIfam; NF008425; PRK11259.1; 1. DR NCBIfam; TIGR01377; soxA_mon; 1. DR PANTHER; PTHR10961:SF7; FAD DEPENDENT OXIDOREDUCTASE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR10961; PEROXISOMAL SARCOSINE OXIDASE; 1. DR Pfam; PF01266; DAO; 1. DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. PE 1: Evidence at protein level; KW Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.1" FT CHAIN 2..389 FT /note="Monomeric sarcosine oxidase" FT /id="PRO_0000213760" FT BINDING 8..38 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255" FT MOD_RES 318 FT /note="S-8alpha-FAD cysteine" FT /evidence="ECO:0000305" FT MUTAGEN 13 FT /note="G->A: Loss of activity." FT /evidence="ECO:0000269|PubMed:8779579" FT MUTAGEN 14 FT /note="A->D,K: Loss of activity." FT /evidence="ECO:0000269|PubMed:8779579" FT MUTAGEN 14 FT /note="A->I,V: Decrease in activity." FT /evidence="ECO:0000269|PubMed:8779579" FT MUTAGEN 14 FT /note="A->L,W,Y: Weak activity." FT /evidence="ECO:0000269|PubMed:8779579" FT MUTAGEN 15 FT /note="G->A: Loss of activity." FT /evidence="ECO:0000269|PubMed:8779579" FT MUTAGEN 16 FT /note="S->P: Weak activity. Loss of activity; when FT associated with G-17." FT /evidence="ECO:0000269|PubMed:8779579" FT MUTAGEN 17 FT /note="M->G: Weak activity. Loss of activity; when FT associated with P-16." FT /evidence="ECO:0000269|PubMed:8779579" FT MUTAGEN 18 FT /note="G->A: Weak activity." FT /evidence="ECO:0000269|PubMed:8779579" FT MUTAGEN 36 FT /note="D->A: Loss of activity." FT /evidence="ECO:0000269|PubMed:8779579" FT MUTAGEN 36 FT /note="D->E: Almost no change in activity." FT /evidence="ECO:0000269|PubMed:8779579" FT MUTAGEN 36 FT /note="D->N: 100-fold decrease in activity." FT /evidence="ECO:0000269|PubMed:8779579" FT MUTAGEN 265 FT /note="C->A,D: Decrease in activity. Stabilizes SoxA FT against chemicals and metal ions." FT /evidence="ECO:0000269|PubMed:7887617" FT MUTAGEN 265 FT /note="C->R,S: Almost no change in activity. Stabilizes FT SoxA against chemicals and metal ions." FT /evidence="ECO:0000269|PubMed:7887617" FT MUTAGEN 318 FT /note="C->S: Weak activity." FT /evidence="ECO:0000269|PubMed:11035956, FT ECO:0000269|PubMed:7887617" FT CONFLICT 39 FT /note="H -> D (in Ref. 2; BAA09716/BAA25926)" FT /evidence="ECO:0000305" FT CONFLICT 316 FT /note="D -> A (in Ref. 2; BAA09716/BAA25926)" FT /evidence="ECO:0000305" SQ SEQUENCE 389 AA; 43294 MW; 77437C4F12B4AC7F CRC64; MSIKKDYDVI VVGAGSMGMA AGYYLSKQGV KTLLVDSFHP PHTNGSHHGD TRIIRHAYGE GREYVPFALR AQELWYELEK ETHHKIFTKT GVLVFGPKGE APFVAETMEA AKEHSLDVDL LEGSEINKRW PGVTVPENYN AIFEKNSGVL FSENCIRAYR ELAEANGAKV LTYTPVEDFE IAEDFVKIQT AYGSFTASKL IVSMGAWNSK LLSKLNIEIP LQPYRQVVGF FECDEKKYSN THGYPAFMVE VPTGIYYGFP SFGGCGLKIG YHTYGQKIDP DTINREFGIY PEDEGNIRKF LETYMPGATG ELKSGDVCMY TKTPDEHFVI DLHPQFSNVA IAAGFSGHGF KFSSVVGETL SQLAVTGKTE HDISIFSINR PALKQKETI //