ID A0A1S3KGK5_LINUN Unreviewed; 363 AA.
AC A0A1S3KGK5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=sarcosine oxidasee (formaldehyde-forming) {ECO:0000256|ARBA:ARBA00012769};
DE EC=1.5.3.1 {ECO:0000256|ARBA:ARBA00012769};
GN Name=LOC106181817 {ECO:0000313|RefSeq:XP_013421768.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013421768.1};
RN [1] {ECO:0000313|RefSeq:XP_013421768.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013421768.1};
RG RefSeq;
RL Submitted (NOV-2023) 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 RefSeq; XP_013421768.1; XM_013566314.2.
DR AlphaFoldDB; A0A1S3KGK5; -.
DR EnsemblMetazoa; XM_013566314.2; XP_013421768.1; LOC106181817.
DR GeneID; 106181817; -.
DR OrthoDB; 1952715at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
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; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..254
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 289..335
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 363 AA; 41594 MW; 2CE00DE40724EC8A CRC64;
MADKNEPEEI RDVIIIGGGI IGCFTAWHLA QQGQRVLLLE QFNHIPHSWG SSAGESRCIR
KAYIEEGYSE LMKKAYEMWT DFENMTQNKF LWKTGMLLVD KGDGRNVKPV KDKLDELGYP
NTTYSSEDLR KHFPTINFKD HIGLFDHDGG VLDVHNIFKS LLLLIDKLGG KIQTGVKVQN
ICPGTEVTLT TNRGKYRAKK VVLTTGPWTA DITKSLELSL PLRVKAATVW FWKEKKFGSY
SLDTGFPVFA DYNIESWNDF IYAVPCYEYP NMLKLHMHHT IEHSIHPDYR DAQMTPDYDF
ILDKHPMWDN IVIGAGFSGH GFKLSPLIGK LLANMVLEKP ITIDMKPFKI SRFQKATWKF
SKL
//
