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Database: UniProt
Entry: A0A238Y7Q2_9ACTN
LinkDB: A0A238Y7Q2_9ACTN
Original site: A0A238Y7Q2_9ACTN 
ID   A0A238Y7Q2_9ACTN        Unreviewed;       375 AA.
AC   A0A238Y7Q2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Glycine oxidase {ECO:0000313|EMBL:SNR67040.1};
GN   ORFNames=SAMN06265355_105315 {ECO:0000313|EMBL:SNR67040.1};
OS   Actinomadura mexicana.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinomadura.
OX   NCBI_TaxID=134959 {ECO:0000313|EMBL:SNR67040.1, ECO:0000313|Proteomes:UP000198420};
RN   [1] {ECO:0000313|EMBL:SNR67040.1, ECO:0000313|Proteomes:UP000198420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44485 {ECO:0000313|EMBL:SNR67040.1,
RC   ECO:0000313|Proteomes:UP000198420};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004948}.
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DR   EMBL; FZNP01000005; SNR67040.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238Y7Q2; -.
DR   OrthoDB; 3214401at2; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000198420; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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;
FT   DOMAIN          3..350
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   375 AA;  39339 MW;  57897CA1F46952E0 CRC64;
     MQIVIIGAGV IGLATAWRTA AGGAAVTLVD PAPASGASSV AAGMLTPVSE LTYGEEPLLR
     LGLASRDRYG AFVAELEELT GLETGYRTDG IIEVAFDSDD LRHLDDLRRF QEDLGIPAEA
     LTGRECRRLE PMLAPGVRGG LLAPEDGSVD PRRLTPALLA ACDRLGVRLV RRRAERVVVE
     DDAAAGVGLD DGTVIRADRV LLAAGPWSGD IGGLPPGTVP PVRPVKGQVI RLRTRAPFLR
     RSTRGLVRGS SVYLVPRADG EIVLGATQEE LGFDTRVTAG GLWELLRDAR ELLPGITELE
     FAEVTAGLRP GSPDNAPVMG PTALPGLLVG TGHFRNGILL TPVSADILSA MLLDGPVPEV
     AGPFAPDRFS PEVSA
//
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