ID MSOX_STRAW Reviewed; 384 AA. AC Q827H4; DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 04-NOV-2008, entry version 39. DE RecName: Full=Monomeric sarcosine oxidase; DE Short=MSOX; DE EC=1.5.3.1; GN Name=soxA; Synonyms=solA; OrderedLocusNames=SAV_6950; OS Streptomyces avermitilis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptomycineae; Streptomycetaceae; Streptomyces. OX NCBI_TaxID=33903; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165; RX MEDLINE=21477403; PubMed=11572948; DOI=10.1073/pnas.211433198; RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., RA Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., RA Kikuchi H., Shiba T., Sakaki Y., Hattori M.; RT "Genome sequence of an industrial microorganism Streptomyces RT avermitilis: deducing the ability of producing secondary RT metabolites."; RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165; RX MEDLINE=22608306; PubMed=12692562; DOI=10.1038/nbt820; RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., RA Sakaki Y., Hattori M., Omura S.; RT "Complete genome sequence and comparative analysis of the industrial RT microorganism Streptomyces avermitilis."; RL Nat. Biotechnol. 21:526-531(2003). CC -!- FUNCTION: Catalyzes the oxidative demethylation of sarcosine (By CC similarity). CC -!- CATALYTIC ACTIVITY: Sarcosine + H(2)O + O(2) = glycine + CC formaldehyde + H(2)O(2). CC -!- COFACTOR: Binds 1 FAD per subunit (By similarity). CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the MSOX/MTOX family. MSOX subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BA000030; BAC74661.1; -; Genomic_DNA. DR RefSeq; NP_828126.1; -. DR HSSP; P40859; 1EL5. DR GeneID; 1211626; -. DR GenomeReviews; BA000030_GR; SAV_6950. DR KEGG; sma:SAV6950; -. DR NMPDR; fig|227882.1.peg.6952; -. DR HOGENOM; Q827H4; -. DR BioCyc; SAVE227882:SAV6950-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:HAMAP. DR GO; GO:0008115; F:sarcosine oxidase activity; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_00516; -; 1. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR Pfam; PF01266; DAO; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; FAD; Flavoprotein; Oxidoreductase. FT CHAIN 1 384 Monomeric sarcosine oxidase. FT /FTId=PRO_0000213763. FT NP_BIND 6 36 FAD (Potential). FT MOD_RES 315 315 S-8alpha-FAD cysteine (By similarity). SQ SEQUENCE 384 AA; 42167 MW; 28302788BB0DE585 CRC64; MSPTYDVIVI GLGGMGSAAA HHLSARGARV LGLEKFGPVH NRGSSHGGSR ITRQSYFEDP AYVPLLLRSY ELYEEVERST GREVATLSGG VMVGRPDSLT VAGSLRSATQ WDLPHEMLDA KEIRRRFPTL NPSNDEVALY EKKAGLVRPE NMVAAHLQLA TRQGAELHFE EPMTRWEPYR DGVRVHTAEN TYTAGQLVIC PGAWAPQLLT DLGVPFTIER QVMYWFQPRH GVGPFRPENH PIYIWEDAEG VQVYGFPSID GPDLGAKVAF FRKGVVCTPE TIDRTVHDHE VQAMADHMSR CIPDLPGTFL KAATCMYSNT PDEHFVIARH PAHPDSVTVA CGFSGHGFKF VPVVGEIVAD LALTGTTAHP IGLFDPRRLA AAPA //