ID A7GLF6_BACCN Unreviewed; 369 AA.
AC A7GLF6;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Glycine oxidase ThiO {ECO:0000313|EMBL:ABS20964.1};
GN OrderedLocusNames=Bcer98_0617 {ECO:0000313|EMBL:ABS20964.1};
OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS20964.1, ECO:0000313|Proteomes:UP000002300};
RN [1] {ECO:0000313|EMBL:ABS20964.1, ECO:0000313|Proteomes:UP000002300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98
RC {ECO:0000313|Proteomes:UP000002300};
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004948}.
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DR EMBL; CP000764; ABS20964.1; -; Genomic_DNA.
DR RefSeq; WP_011983720.1; NC_009674.1.
DR AlphaFoldDB; A7GLF6; -.
DR STRING; 315749.Bcer98_0617; -.
DR GeneID; 56416206; -.
DR KEGG; bcy:Bcer98_0617; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_4_5_9; -.
DR OrthoDB; 9794226at2; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000002300; 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;
FT DOMAIN 6..350
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 369 AA; 41201 MW; 43CF0D098269D550 CRC64;
MSKKYDVAII GGGVIGSSVA HFLAERSCHV AIVEKQRVAS EASKAAAGLL GVQAEWDVYN
PLFELARESR AIFPQLAKAL REKTGIDIGY EEKGIYRIAQ NEEEKTRIRN IMNWQQETGE
ESYFLTGDEL RQKEPFLSSS IIGAVYYPKD GHVIAPELTK AFAHSAAISG TDIYEQTEVF
DIRVEKNRVC GIVTSEGFIS CEKVVIAGGS WSTKLLQYFH RDWGTYPVKG EVVAVKSYKP
LVRAPIFQDR FYIAPKRGGR YVIGATMKPH TFNKSVQPKS IISILERAYS ILPALKDAEW
ETAWAGLRPQ SNHDVPYMGE HEEIKGLYAC TGHYRNGILL SPISGQYMAD IIEGKQTNHL
LDSLFSKSV
//
