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Database: UniProt
Entry: A0A0X3V454_9ACTN
LinkDB: A0A0X3V454_9ACTN
Original site: A0A0X3V454_9ACTN 
ID   A0A0X3V454_9ACTN        Unreviewed;       388 AA.
AC   A0A0X3V454;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Glycine oxidase {ECO:0000313|EMBL:KUL39237.1};
GN   ORFNames=ADL12_15950 {ECO:0000313|EMBL:KUL39237.1};
OS   Streptomyces regalis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=68262 {ECO:0000313|EMBL:KUL39237.1, ECO:0000313|Proteomes:UP000053923};
RN   [1] {ECO:0000313|Proteomes:UP000053923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3151 {ECO:0000313|Proteomes:UP000053923};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004948}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUL39237.1}.
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DR   EMBL; LLZG01000104; KUL39237.1; -; Genomic_DNA.
DR   RefSeq; WP_062702952.1; NZ_LLZG01000104.1.
DR   AlphaFoldDB; A0A0X3V454; -.
DR   OrthoDB; 3214401at2; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000053923; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053923}.
FT   DOMAIN          8..359
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   388 AA;  41143 MW;  E07393B621A7DDF0 CRC64;
     MSRTRTSDVL VIGGGIIGLV TAWRAAQRGF TTAVVDPEPG GGAAQVAAGM LAAVTELHYG
     EQTLLGLNLA SARRYPDFAA ELTDLTGHDL GYRRCGTLAV ALDSDDRAHL RELHALQRRS
     GLDSEWLSGR ECRRLEPMLA PGVRGGLRVD GDHQIDPRRL AGALVAACER AGVVFHRTWA
     ERFDVVRDRA AGVTTANGTE LGAGQVVLAA GSLSGRLTGV PDHVLPPVRP VKGQVLRLTV
     PKRYAPFLSR TVRAVVRGSQ VYLVPRESGE LVVGATSEEL GWDTTVTAGG VYELLRDAHE
     LVPGITELPL TETRAGLRPG SPDNAPLLGP TELDGLLLAT GHYRNGVLLT PVTGDAMAHA
     LTTGELPDEA RPFTPKRFSA AALTEQPA
//
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