ID SOXB_CORS1 Reviewed; 405 AA. AC P40875; Q46335; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 25-NOV-2008, entry version 65. DE RecName: Full=Sarcosine oxidase subunit beta; DE Short=Sarcosine oxidase subunit B; DE EC=1.5.3.1; GN Name=soxB; OS Corynebacterium sp. (strain P-1). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=69006; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=95355441; PubMed=7543100; DOI=10.1074/jbc.270.31.18252; RA Chlumsky L.J., Zhang L., Jorns M.S.; RT "Sequence analysis of sarcosine oxidase and nearby genes reveals RT homologies with key enzymes of folate one-carbon metabolism."; RL J. Biol. Chem. 270:18252-18259(1995). RN [2] RP PROTEIN SEQUENCE OF 161-187 AND 334-404. RC STRAIN=U-96; RX MEDLINE=92041745; PubMed=1939012; RA Suzuki H., Kawamura-Konishi Y.; RT "Cysteine residues in the active site of Corynebacterium sarcosine RT oxidase."; RL J. Biochem. 109:909-917(1991). RN [3] RP PARTIAL PROTEIN SEQUENCE. RC STRAIN=U-96; RX MEDLINE=89076343; PubMed=3202887; RA Suzuki H., Kawamura-Konishi Y.; RT "Presence of AMP binding sequence in subunit B of Corynebacterium RT sarcosine oxidase."; RL Biochem. Int. 17:577-583(1988). RN [4] RP CHARACTERIZATION. RX MEDLINE=94032225; PubMed=7692961; DOI=10.1021/bi00092a024; RA Chlumsky L.J., Zhang L., Ramsey A.J., Jorns M.S.; RT "Preparation and properties of recombinant corynebacterial sarcosine RT oxidase: evidence for posttranslational modification during turnover RT with sarcosine."; RL Biochemistry 32:11132-11142(1993). RN [5] RP FMN-BINDING. RX PubMed=8611516; DOI=10.1021/bi952995h; RA Willie A., Edmondson D.E., Jorns M.S.; RT "Sarcosine oxidase contains a novel covalently bound FMN."; RL Biochemistry 35:5292-5299(1996). RN [6] RP PROTEIN SEQUENCE OF 174-178, FMN-BINDING AT HIS-173, AND MASS RP SPECTROMETRY. RX PubMed=9485355; DOI=10.1021/bi972705s; RA Chlumsky L.J., Sturgess A.W., Nieves E., Jorns M.S.; RT "Identification of the covalent flavin attachment site in sarcosine RT oxidase."; RL Biochemistry 37:2089-2095(1998). RN [7] RP PROTEIN SEQUENCE OF 174-178, FMN-BINDING AT HIS-173, AND MASS RP SPECTROMETRY. RX PubMed=11902668; DOI=10.1023/A:1014135216860; RA Mukouyama E.B., Ohsawa H., Suzuki H.; RT "Cofactors in sarcosine oxidase from Corynebacterium sp. U-96."; RL J. Protein Chem. 21:59-64(2002). CC -!- FUNCTION: Catalyzes the oxidative demethylation of sarcosine to CC yield glycine, hydrogen peroxide and 5,10- CC methylenetetrahydrofolate. CC -!- CATALYTIC ACTIVITY: Sarcosine + H(2)O + O(2) = glycine + CC formaldehyde + H(2)O(2). CC -!- COFACTOR: Binds 1 FAD per subunit. CC -!- COFACTOR: Binds 1 FMN covalently. CC -!- SUBUNIT: Heterotetramer (alpha 100 kDa, beta 42 kDa, gamma 20 kDa, CC and delta 6 kDa). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the soxB family. 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; U23955; AAC43459.1; -; Genomic_DNA. DR PIR; PX0049; PX0049. DR SMR; P40875; 3-405. DR BioCyc; MetaCyc:MON-8522; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0008115; F:sarcosine oxidase activity; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0046653; P:tetrahydrofolate metabolic process; IEA:InterPro. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR InterPro; IPR006278; SoxB. DR Pfam; PF01266; DAO; 1. DR TIGRFAMs; TIGR01373; soxB; 1. PE 1: Evidence at protein level; KW Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; FMN; KW Oxidoreductase. FT CHAIN 1 405 Sarcosine oxidase subunit beta. FT /FTId=PRO_0000072044. FT MOD_RES 173 173 Tele-8alpha-FMN histidine. FT VARIANT 167 167 R -> Y (in strain: U-96). FT VARIANT 172 173 KH -> CK (in strain: U-96). FT VARIANT 178 178 W -> T (in strain: U-96). FT VARIANT 182 182 R -> N (in strain: U-96). FT VARIANT 359 359 K -> FC (in strain: U-96). FT VARIANT 366 366 F -> Y (in strain: U-96). FT VARIANT 370 370 H -> E (in strain: U-96). FT VARIANT 374 374 N -> A (in strain: U-96). FT VARIANT 377 379 AHA -> PKK (in strain: U-96). FT VARIANT 385 385 S -> A (in strain: U-96). SQ SEQUENCE 405 AA; 43987 MW; 401141810BA60CDE CRC64; MADLLPEHPE FLWANPEPKK SYDVVIVGGG GHGLATAYYL AKNHGITNVA VLEKGWLAGG NMARNTTIIR SNYLWDESAG IYEKSLKLWE QLPEELDYDF LFSQRGVLNL AHTLGDVRES VRRVEANKFN GVDAEWLTPE QVKEVCPIIN IGDDIRYPVM GATYQPRAGI AKHDHVAWAF ARKANEMGVD IIQNCEVTGF LKDGEKVTGV KTTRGTIHAG KVALAGAGHS SVLAELAGFE LPIQSHPLQA LVSELFEPVH PTVVMSNHIH VYVSQAHKGE LVMGAGIDSY NGYGQRGAFH VIEEQMAAAV ELFPIFARAH VLRTWGGIVD TTMDASPIIS KTPIQNLYVN CGWGTGGFKG TPGAGFTLAH TIANDEAHAL NAPFSLERFE TGHLIDEHGA AAVAH //