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Database: UniProt
Entry: Q82AG3_STRAW
LinkDB: Q82AG3_STRAW
Original site: Q82AG3_STRAW 
ID   Q82AG3_STRAW            Unreviewed;       388 AA.
AC   Q82AG3;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   SubName: Full=Glycine oxidase {ECO:0000313|EMBL:BAC73806.1};
GN   Name=goxB {ECO:0000313|EMBL:BAC73806.1};
GN   ORFNames=SAVERM_6095 {ECO:0000313|EMBL:BAC73806.1};
OS   Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS   14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=227882 {ECO:0000313|EMBL:BAC73806.1, ECO:0000313|Proteomes:UP000000428};
RN   [1] {ECO:0000313|EMBL:BAC73806.1, ECO:0000313|Proteomes:UP000000428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC   NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX   PubMed=11572948; DOI=10.1073/pnas.211433198;
RA   Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA   Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M.;
RT   "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT   deducing the ability of producing secondary metabolites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN   [2] {ECO:0000313|EMBL:BAC73806.1, ECO:0000313|Proteomes:UP000000428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC   NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX   PubMed=12692562; DOI=10.1038/nbt820;
RA   Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M., Omura S.;
RT   "Complete genome sequence and comparative analysis of the industrial
RT   microorganism Streptomyces avermitilis.";
RL   Nat. Biotechnol. 21:526-531(2003).
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004948}.
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DR   EMBL; BA000030; BAC73806.1; -; Genomic_DNA.
DR   RefSeq; WP_010987496.1; NZ_JZJK01000089.1.
DR   AlphaFoldDB; Q82AG3; -.
DR   KEGG; sma:SAVERM_6095; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_4_5_11; -.
DR   OrthoDB; 3214401at2; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000000428; Chromosome.
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:UP000000428}.
FT   DOMAIN          8..359
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   388 AA;  41136 MW;  A42FEE951DFB408A CRC64;
     MSPTHTSDVL VVGGGIIGLV TAWRAAQRGF ATAVVDPDPG GGAAQVAAGM LAAVTELHYG
     EQTLLGLNLA SARRYPDFAA ELTEATGHDL GYRRCGTLAV ALDADDRAQL RELHALQRRS
     GLESEWLNGR ECRRLEPMLA PGVRGGLRVD GDHQIDPRRL AKALVVACER AGVVFHRVWA
     ERLFLVRGRA AGVVTRDGAE LAAGQIVLAG GSLSGQLAGV PDDVLPPVRP VKGQVLRLTV
     PKRYAPFLSR TVRAVVRGSQ IYLVPRESGE LVVGATSEEL GWDTTVTAGG VYELLRDAHE
     LVPGITELPL TETRAGLRPG SPDNAPLLGP TELDGLLLAT GHFRNGVLLT PVTGDAMAHV
     LTTGELPDEA RPFTPRRFST AVLTEQSA
//
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