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Database: UniProt
Entry: M2Y249_GALSU
LinkDB: M2Y249_GALSU
Original site: M2Y249_GALSU 
ID   M2Y249_GALSU            Unreviewed;       618 AA.
AC   M2Y249;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Glycine oxidase ThiO {ECO:0000313|EMBL:EME30048.1};
DE            EC=1.4.3.19 {ECO:0000313|EMBL:EME30048.1};
GN   ORFNames=Gasu_26340 {ECO:0000313|EMBL:EME30048.1};
OS   Galdieria sulphuraria (Red alga).
OC   Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC   Galdieria.
OX   NCBI_TaxID=130081 {ECO:0000313|EMBL:EME30048.1, ECO:0000313|Proteomes:UP000030680};
RN   [1] {ECO:0000313|Proteomes:UP000030680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX   PubMed=23471408; DOI=10.1126/science.1231707;
RA   Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA   Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA   Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA   Lercher M.J., Weber A.P.;
RT   "Gene transfer from bacteria and archaea facilitated evolution of an
RT   extremophilic eukaryote.";
RL   Science 339:1207-1210(2013).
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004948}.
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DR   EMBL; KB454503; EME30048.1; -; Genomic_DNA.
DR   RefSeq; XP_005706568.1; XM_005706511.1.
DR   AlphaFoldDB; M2Y249; -.
DR   STRING; 130081.M2Y249; -.
DR   EnsemblPlants; EME30048; EME30048; Gasu_26340.
DR   GeneID; 17088807; -.
DR   Gramene; EME30048; EME30048; Gasu_26340.
DR   KEGG; gsl:Gasu_26340; -.
DR   OrthoDB; 298051at2759; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000030680; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0043799; F:glycine oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR012727; Gly_oxidase_ThiO.
DR   NCBIfam; TIGR02352; thiamin_ThiO; 1.
DR   PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR13847:SF293; TRNA 5-METHYLAMINOMETHYL-2-THIOURIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN MNMC; 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.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:EME30048.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030680}.
FT   DOMAIN          36..370
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   REGION          563..595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..585
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   618 AA;  68715 MW;  780C8343F46CF543 CRC64;
     MEQYRSTRNC IFRRRNVFYS LNSCRHIQTS TKHSSDLIVI GGGLIGLSIA WEAAKLGAKI
     TVVVGDGNAS ATVAAAGMLA PQGERLEQSA LLKLCVSSRS LYPAFVEEVE RTSGMSTDFS
     SSGFICPSFG DDAVSTWKPP IQGGHHQWLS KKELLLFEPL LSEEVVGGWW FPEDCHINNK
     KLYESLTVAC KRIGVQFIYS FVANMIYSNN MLSKLQLSTG DVIAGERYVV ANGCWLRKLI
     PLPVHPQKGQ MISLCNENGL VPLQRVIYGE GGYIVPRKNG EIVLGATVED NCLVDFKTSA
     GGIYTVLEET FKLIPSLSQL PLRDTWTGYR PTTPDLLPIF GKLWFENVSV CAGHHRNGIL
     LAPISGKIAS RVALDMSMDD IILESDIINA FSVQRFSHAS ASNWNKIQNV EDYNDMDEKG
     VTTEELKSLS SESQKLWKDL SKKQEIEDSS EVKLWQVGED GQLIPIHYRQ PPADLFNTKG
     YGDFTDQNFA ISQTAQSNSS HLNGVLSEVE RQYSSTKDSA TTEWSQSTDA YLDISSGVGD
     DNYEREFRKA ILANLHFQAP VSERTDLSPS SSLDKSLTNE TCQSDQEEEN GVEKGLEDDY
     NQWLKLYETV DTNQNIPC
//
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