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SOXB_CORS1
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   03-AUG-2022, entry version 108.
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; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium; unclassified Corynebacterium.
OX   NCBI_TaxID=69006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-36.
RX   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 homologies
RT   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   PubMed=1939012; DOI=10.1093/oxfordjournals.jbchem.a123479;
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   PubMed=3202887;
RA   Suzuki H., Kawamura-Konishi Y.;
RT   "Presence of AMP binding sequence in subunit B of Corynebacterium sarcosine
RT   oxidase.";
RL   Biochem. Int. 17:577-583(1988).
RN   [4]
RP   CHARACTERIZATION, AND MUTAGENESIS OF HIS-175.
RX   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 with
RT   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 IDENTIFICATION BY
RP   MASS 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 IDENTIFICATION BY
RP   MASS 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 yield
CC       glycine, hydrogen peroxide and 5,10-methylenetetrahydrofolate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O2 + sarcosine = 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   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC       Note=Binds 1 FMN covalently.;
CC   -!- SUBUNIT: Heterotetramer (SoxA, SoxB, SoxG and SoxD).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the SoxB family. {ECO:0000305}.
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DR   EMBL; U23955; AAC43459.1; -; Genomic_DNA.
DR   PIR; PX0049; PX0049.
DR   AlphaFoldDB; P40875; -.
DR   SMR; P40875; -.
DR   KEGG; ag:AAC43459; -.
DR   BioCyc; MetaCyc:MON-8522; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008115; F:sarcosine oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046653; P:tetrahydrofolate metabolic process; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR006278; SoxB.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR01373; soxB; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; FMN;
KW   Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7543100"
FT   CHAIN           2..405
FT                   /note="Sarcosine oxidase subunit beta"
FT                   /id="PRO_0000072044"
FT   REGION          23..53
FT                   /note="ADP binding"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         173
FT                   /note="Tele-8alpha-FMN histidine"
FT   VARIANT         167
FT                   /note="R -> Y (in strain: U-96)"
FT   VARIANT         172..173
FT                   /note="KH -> CK (in strain: U-96)"
FT   VARIANT         178
FT                   /note="W -> T (in strain: U-96)"
FT   VARIANT         182
FT                   /note="R -> N (in strain: U-96)"
FT   VARIANT         359
FT                   /note="K -> FC (in strain: U-96)"
FT   VARIANT         366
FT                   /note="F -> Y (in strain: U-96)"
FT   VARIANT         370
FT                   /note="H -> E (in strain: U-96)"
FT   VARIANT         374
FT                   /note="N -> A (in strain: U-96)"
FT   VARIANT         377..379
FT                   /note="AHA -> PKK (in strain: U-96)"
FT   VARIANT         385
FT                   /note="S -> A (in strain: U-96)"
FT   MUTAGEN         175
FT                   /note="H->A: No effect on FMN binding."
FT                   /evidence="ECO:0000269|PubMed:7692961"
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
 
 
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