ID A0A0P7YC94_9RHOB Unreviewed; 417 AA.
AC A0A0P7YC94;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 Name=soxB {ECO:0000313|EMBL:KPP85773.1};
GN ORFNames=HLUCCO07_01615 {ECO:0000313|EMBL:KPP85773.1};
OS Rhodobacteraceae bacterium HLUCCO07.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666914 {ECO:0000313|EMBL:KPP85773.1, ECO:0000313|Proteomes:UP000050369};
RN [1] {ECO:0000313|EMBL:KPP85773.1, ECO:0000313|Proteomes:UP000050369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCO07 {ECO:0000313|EMBL:KPP85773.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:KPP85773.1}.
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DR EMBL; LJSU01000019; KPP85773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7YC94; -.
DR STRING; 1666914.HLUCCO07_01615; -.
DR PATRIC; fig|1666914.4.peg.881; -.
DR Proteomes; UP000050369; Unassembled WGS sequence.
DR GO; GO:0008115; F:sarcosine oxidase activity; IEA:UniProtKB-EC.
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 Oxidoreductase {ECO:0000313|EMBL:KPP85773.1}.
FT DOMAIN 35..78
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 417 AA; 45430 MW; F94CFE4263F47756 CRC64;
MRFSALKILT EGLTGNKGWT PHWRDPEPKA EYDAIVIGGG GHGLSTAYYL AKNHGLRNVA
VLEKGYIGGG NVGRNTTIVR ANYFLPGNSE FYSHSLKLWE GLEEDLNYNV MHSQRGLINL
FHSDGQRDAF ARRGNAMINQ GDDAILLDRD GVREILPYLD FDNARFPIYG GLYHPRGGTA
RHDAVAWGYA RGADQRGVDL IQNCEVTGID IENGQVRGVQ TTRGAIRAKK VGLVVAGRSS
QVAAMAGMRL PIESHVLQAF VTEGLKPVID HVVSFGMGHF YISQSDKGGL VFGGDIDFYA
SYAQRGNLPM AEHVMEAGMA LMPMIGKARV LRSWGGIMDM SPDGSPVIDA THIDGLFLNC
GWCYGGFKAV PASGWCMAYL MATGTPHEHA AGFRLDRFET GRGLMDEEGT GAQHNLH
//
