ID A0A2M9ISS7_9ACTN Unreviewed; 406 AA.
AC A0A2M9ISS7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Sarcosine oxidase subunit beta {ECO:0000256|ARBA:ARBA00044150};
DE EC=1.5.3.24 {ECO:0000256|ARBA:ARBA00044044};
DE AltName: Full=Sarcosine oxidase (5,10-methylenetetrahydrofolate-forming) subunit beta {ECO:0000256|ARBA:ARBA00044216};
DE AltName: Full=Tetrameric sarcosine oxidase subunit beta {ECO:0000256|ARBA:ARBA00044295};
GN ORFNames=CG719_02000 {ECO:0000313|EMBL:PJM97685.1};
OS Streptomyces sp. CB01373.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2020325 {ECO:0000313|EMBL:PJM97685.1, ECO:0000313|Proteomes:UP000232070};
RN [1] {ECO:0000313|Proteomes:UP000232070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01373 {ECO:0000313|Proteomes:UP000232070};
RA Pan G., Xu Z., Guo Z., Ma M., Yang D., Zhou H., Gansemans Y., Zhu X.,
RA Zhao L.-X., Jiang Y., Cheng J., van Nieuwerburgh F., Suh J.W., Duan Y.,
RA Shen B.;
RT "Discovery of the Leinamycin Family of Natural Products by Mining
RT Actinobacterial Genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:0-0(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + O2 + sarcosine = (6R)-5,10-
CC methylene-5,6,7,8-tetrahydrofolate + glycine + H2O2;
CC Xref=Rhea:RHEA:70455, ChEBI:CHEBI:15379, ChEBI:CHEBI:15636,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:57305, ChEBI:CHEBI:57433,
CC ChEBI:CHEBI:57453; EC=1.5.3.24;
CC Evidence={ECO:0000256|ARBA:ARBA00043745};
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; Evidence={ECO:0000256|ARBA:ARBA00043809};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the SoxB family.
CC {ECO:0000256|ARBA:ARBA00043973}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PJM97685.1}.
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DR EMBL; NNBK01000001; PJM97685.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9ISS7; -.
DR OrthoDB; 9805852at2; -.
DR Proteomes; UP000232070; Unassembled WGS sequence.
DR GO; GO:0008115; F:sarcosine oxidase activity; IEA:InterPro.
DR GO; GO:0046653; P:tetrahydrofolate metabolic process; IEA:InterPro.
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 InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR006278; SoxB.
DR NCBIfam; TIGR01373; soxB; 1.
DR PANTHER; PTHR13847:SF287; FAD-DEPENDENT OXIDOREDUCTASE DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 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.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022643};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Reference proteome {ECO:0000313|Proteomes:UP000232070}.
FT DOMAIN 25..69
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 406 AA; 43993 MW; E711E995B26064D8 CRC64;
MTAAPLPEHP DWLWRTPDPR PSYDVVIVGA GGHGLATAYY LAKNHGITNV AVLEKGWLAG
GNMARNTTII RSNYLWDESA AIYEHALKLW ERLPEELDYD FLFSQRGVLN LAHTLQDVRE
GVRRVNANRL NGVDAEWLET DEVAKVCPIV NVSPGTRYPV LGGTYQPRAG IAKHDHVAWA
LARRADEMGV DLIQNCEVTG FVKDGDRVVG VETSRGRILA GRVGLAAAGH SSVLAERAGF
RLPVQSHPLQ ALVSELHQPV HPTVVMSNHV HVYVSQAHKG ELVMGAGVDT YNGYGQRGSF
HVIEHQMAAA VELFPVFARA HVLRTWGGIV DVTPDASPVI GTTPVENLFV NCGWGTGGFK
ATPAAGWTFA HTIATGEPHP LNKPFALERF TTGALIDEHG AAAVAH
//
