MSOX_STRSB
ID MSOX_STRSB Reviewed; 389 AA.
AC P40854;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Monomeric sarcosine oxidase {ECO:0000255|HAMAP-Rule:MF_00516};
DE Short=MSOX {ECO:0000255|HAMAP-Rule:MF_00516};
DE EC=1.5.3.1 {ECO:0000255|HAMAP-Rule:MF_00516};
GN Name=soxA {ECO:0000255|HAMAP-Rule:MF_00516};
OS Streptomyces sp. (strain KB210-8SY).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=72592;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-31; 122-143;
RP 230-259 AND 268-283.
RX PubMed=1368326; DOI=10.1271/bbb.56.432;
RA Suzuki K., Ogishima M., Sugiyama M., Inouye Y., Nakamura S., Imamura S.;
RT "Molecular cloning and expression of a Streptomyces sarcosine oxidase gene
RT in Streptomyces lividans.";
RL Biosci. Biotechnol. Biochem. 56:432-436(1992).
CC -!- FUNCTION: Catalyzes the oxidative demethylation of sarcosine.
CC {ECO:0000255|HAMAP-Rule:MF_00516}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00516};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00516};
CC Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_00516};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00516}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00516}.
CC -!- SIMILARITY: Belongs to the MSOX/MTOX family. MSOX subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00516}.
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DR EMBL; S39464; AAC60412.2; -; Genomic_DNA.
DR EMBL; D10623; BAA01473.1; -; Genomic_DNA.
DR AlphaFoldDB; P40854; -.
DR SMR; P40854; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0008115; F:sarcosine oxidase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.50.60; -; 1.
DR HAMAP; MF_00516; MSOX; 1.
DR InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR045170; MTOX.
DR InterPro; IPR006281; SoxA_mon.
DR PANTHER; PTHR10961; PTHR10961; 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1368326"
FT CHAIN 2..389
FT /note="Monomeric sarcosine oxidase"
FT /id="PRO_0000213764"
FT BINDING 6..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00516"
FT MOD_RES 315
FT /note="S-8alpha-FAD cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00516"
SQ SEQUENCE 389 AA; 42263 MW; EFE480AF4C1B73E6 CRC64;
MSPTYDVIVI GLGGMGSAAA HHLSARGARV LGLEKFGPVH NRGSSHGGSR ITRQSYFEDP
AYVPLLLRAY ELYEELERAT GRNVATLCGG VMAGPPDSRT VSGSLRSATE WDLAHEMLDA
KEIRRRFPTL APDDDEVALF EAKAGLLRPE NMVAAHLQLA TRQGAELRFE EPVLRWEPYR
DGVRVHTGEN TYTAGQLVIC PGAWAPQLLA DIGVPITVER QIMYWFQPKG GTGPFVPERH
PVYIWEDADG VQVYGFPAID GPEKGAKVAF FRKGQHTTPE TIDRTVHAHE VRAMADHMSA
LIPDLPGTFL KAATCMYSNT PDEHFVIARH PAHPESVTVA CGFSGHGFKF VPVVGEILAD
LALTGATAHP IGLFDPARLT APAARGVQP
