ID A0A1I8IG67_9PLAT Unreviewed; 666 AA.
AC A0A1I8IG67;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=sarcosine oxidasee (formaldehyde-forming) {ECO:0000256|ARBA:ARBA00012769};
DE EC=1.5.3.1 {ECO:0000256|ARBA:ARBA00012769};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0012535-snap-gene-0.1-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0012535-snap-gene-0.1-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00000323};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the MSOX/MTOX family.
CC {ECO:0000256|ARBA:ARBA00010989}.
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DR AlphaFoldDB; A0A1I8IG67; -.
DR WBParaSite; maker-uti_cns_0012535-snap-gene-0.1-mRNA-1; maker-uti_cns_0012535-snap-gene-0.1-mRNA-1; maker-uti_cns_0012535-snap-gene-0.1.
DR Proteomes; UP000095280; Unplaced.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 2.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR045170; MTOX.
DR PANTHER; PTHR10961; PEROXISOMAL SARCOSINE OXIDASE; 1.
DR PANTHER; PTHR10961:SF7; PEROXISOMAL SARCOSINE OXIDASE; 1.
DR Pfam; PF01266; DAO; 2.
DR SUPFAM; SSF58113; Apolipoprotein A-I; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}.
FT DOMAIN 12..127
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 128..338
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT REGION 388..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 457..580
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 388..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 666 AA; 72763 MW; 35E09431DFC161DE CRC64;
AAAAQQQQRQ QHVAVVGCGV NGLCTAWQLL ERGHRVTLLE QFPVPHSRGS SHGHSRITRY
AYKEAEYARL MRRAFPLWSR LESLSGQRLF INCGMASLGS GAYLRNISEV LESNSMPLER
LSGQSLASRC LQALRSRVAQ LGGRLRDCVR VTAIEPQPDG SVRLRLSGSG TAAAASAEEL
TADSVVLAAG AWAGQLLSGL GLELPLRPIG VTAMYWRLRR GEGAAETGDF GPEKFPTFDY
QDKDFHVYGL PELEYPGMIC MHDGPDLDPD IRETREQREP YYLPELTDFV RRWFPHLVPE
PAVTEKCIYT LTPDRGLIVD RHPKHRNILF VCGCSVIGQL LSEMATGQPP SEDLAFMSAG
RFKHAEIQMA TSSPDSISHV ADGLSETATA KSSNISDSKA SPSASSVGNK KKPQSSANAK
LDRIEAGINQ IIHQLAGKAA SSIDAKAGPQ AESPDTSTNW RRLAEELQET IDSLAARLET
QAAQLESVQE EAQRQRETAE AENRDLRRRL LSFRRQLDAS QTARARLSAD LSKVQAELAE
LKQSAAGAGA AGNSDMEETV EALTAQLDRS NEQLEQVLLT RSCSCDQRLH DCCRREGGLD
SQFRSKRSYE TVRTSGGRYG GSEDGTAHGP QQAAQASAAA DRKSKIRSPN KSSTKRDVKS
KEGKQK
//
