ID A0A0C4WQC1_9GAMM Unreviewed; 381 AA.
AC A0A0C4WQC1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=FAD-dependent glycine oxidase {ECO:0000313|EMBL:AJE20462.1};
GN Name=thiO {ECO:0000313|EMBL:AJE20462.1};
GN ORFNames=Achr_9800 {ECO:0000313|EMBL:AJE20462.1};
OS Azotobacter chroococcum NCIMB 8003.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=1328314 {ECO:0000313|EMBL:AJE20462.1, ECO:0000313|Proteomes:UP000068210};
RN [1] {ECO:0000313|EMBL:AJE20462.1, ECO:0000313|Proteomes:UP000068210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 8003 {ECO:0000313|EMBL:AJE20462.1,
RC ECO:0000313|Proteomes:UP000068210};
RX PubMed=26061173;
RA Robson R.L., Jones R., Robson R.M., Schwartz A., Richardson T.H.;
RT "Azotobacter Genomes: The Genome of Azotobacter chroococcum NCIMB 8003
RT (ATCC 4412).";
RL PLoS ONE 10:E0127997-E0127997(2015).
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004948}.
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DR EMBL; CP010415; AJE20462.1; -; Genomic_DNA.
DR RefSeq; WP_052263866.1; NZ_CP010415.1.
DR AlphaFoldDB; A0A0C4WQC1; -.
DR STRING; 1328314.Achr_9800; -.
DR KEGG; acx:Achr_9800; -.
DR HOGENOM; CLU_007884_4_5_6; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000068210; 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:UP000068210}.
FT DOMAIN 2..343
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 381 AA; 40540 MW; 398845C6BC086DE8 CRC64;
MRVLVVGGGA IGMLSALRLA EAGLEVRLLD QGSLGRESSW AGGGIVSPLY PWRYSPAVTA
LAHWSQDFYP ALGERLRQET GIDPEVHVTG LYWLDLEDEA EALAWAAREG RPLAAVDIDA
VHKAVPALGP GFSRALFMPG VANVRNPRLL AALREALARL PNVTLEENLP VTGFVREGER
VVGVRTASGE WRADRVVVAA GAWSGELLAT LGLELPVKPM KGQMILYKCA EDFLPRMVMA
DGRYAIPRRD GHILVGSTLE DVGFDKTPTG EALESLKASA EALLPALAGA EVVKQWAGLR
PGSPEGIPYI GPVPGFEGLW LNCGHFRNGL VLAPASCELL ADLLLAREPI VDPAPYAPAG
RIGRGMAGCT RPTGYSHGSD V
//
