ID G2J1M4_PSEUL Unreviewed; 417 AA.
AC G2J1M4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
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:BAK76202.1};
GN OrderedLocusNames=NH8B_1380 {ECO:0000313|EMBL:BAK76202.1};
OS Pseudogulbenkiania sp. (strain NH8B).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Pseudogulbenkiania.
OX NCBI_TaxID=748280 {ECO:0000313|EMBL:BAK76202.1, ECO:0000313|Proteomes:UP000001274};
RN [1] {ECO:0000313|Proteomes:UP000001274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NH8B {ECO:0000313|Proteomes:UP000001274};
RX PubMed=22038961; DOI=10.1128/JB.06127-11;
RA Ishii S., Tago T., Nishizawa T., Oshima K., Hattori M., Senoo K.;
RT "Complete genome sequence of the denitrifying and N(2)O-reducing bacterium
RT Pseudogulbenkiania sp. strain NH8B.";
RL J. Bacteriol. 193:6395-6396(2011).
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}.
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DR EMBL; AP012224; BAK76202.1; -; Genomic_DNA.
DR RefSeq; WP_008955494.1; NC_016002.1.
DR AlphaFoldDB; G2J1M4; -.
DR STRING; 748280.NH8B_1380; -.
DR KEGG; pse:NH8B_1380; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_4_1_4; -.
DR OrthoDB; 9342835at2; -.
DR Proteomes; UP000001274; Chromosome.
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; 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:UP000001274}.
FT DOMAIN 36..80
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 417 AA; 45228 MW; 0D1BD9CF8A5EDF40 CRC64;
MANRYSLWSL LKNGLKHNES WQPAWRSPQA KPRYDVIIVG GGGHGLATAY YLAKNHGVKN
VAVLEKGYLG GGNTARNTTI VRSNYLWDEA AQLYEHAMKL WEGLSLDLNF NVMFSQRGVM
NLGHTLQDMR DIERRVNANN LNGIDGVVLS PKEIQDIVPL MDISAKTRYP VMGASYQPRG
GVARHDAVAW GFARGASELG VDIIEQCEVI DMIIEDGRIK GVKTTKGDIF ADRVGCVAAG
NSTPLAKMAG VRLPLESHPL QAFVSESMKP CLDTVVMSNA VHGYVSQSDK GELVIGAGID
SYLGYGQRGS PHVIEHTAAA IIELFPSFSR VRMNRQWGGI VDVAPDACPI ISKTKVKGLY
FNCGWGTGGF KATPGSGYVF AHTIANDEAH PLNKAFALDR FNTGHLIDEH GAAGVAH
//
