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
//