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Database: UniProt
Entry: A0A0M2SVY3_9BACI
LinkDB: A0A0M2SVY3_9BACI
Original site: A0A0M2SVY3_9BACI 
ID   A0A0M2SVY3_9BACI        Unreviewed;       374 AA.
AC   A0A0M2SVY3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Glycine oxidase {ECO:0000313|EMBL:KKK37127.1};
GN   ORFNames=WQ57_15490 {ECO:0000313|EMBL:KKK37127.1};
OS   Mesobacillus campisalis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX   NCBI_TaxID=1408103 {ECO:0000313|EMBL:KKK37127.1, ECO:0000313|Proteomes:UP000034166};
RN   [1] {ECO:0000313|EMBL:KKK37127.1, ECO:0000313|Proteomes:UP000034166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA2-6 {ECO:0000313|EMBL:KKK37127.1,
RC   ECO:0000313|Proteomes:UP000034166};
RA   Mathan Kumar R., Kaur G., Kumar A., Singh N.K., Kaur N., Kumar N.,
RA   Mayilraj S.;
RT   "Taxonomic description and genome sequence of Bacillus campisalis sp. nov.,
RT   a novel member of the genus Bacillus isolated from solar saltern.";
RL   Submitted (APR-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:KKK37127.1}.
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DR   EMBL; LAYY01000017; KKK37127.1; -; Genomic_DNA.
DR   RefSeq; WP_046524670.1; NZ_LAYY01000017.1.
DR   AlphaFoldDB; A0A0M2SVY3; -.
DR   PATRIC; fig|1408103.3.peg.3457; -.
DR   OrthoDB; 9794226at2; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000034166; 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:UP000034166}.
FT   DOMAIN          7..351
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   374 AA;  40583 MW;  4112349DB71E7DDB CRC64;
     MTYIYDSIIV GGGVIGGSIA FHLARRGKKV LLLEKNVLAG ESSRAAAGML GAQAELESSS
     PLFPLAKKSR EMFPNIAAAL KELSGMDIEL VNKGMFKVAL NDEQAEELKR KVEIHRSHGE
     QADWLSAEDV KNHEPLLSHS VLGAMFLPKD GQVSAHRLSL AFFSAAAVLG AEVKEFAAVH
     TFLIEKDRVN GVRTNCGDYF SENVIVASGA WSAELLKDFG MVLDTYPVKG ECFSVVTTRP
     LLEKTIFAKG CYLVPKAGGR TIVGATEHPH TFNKKVSVAG VFSLMDKARR IVPSIVDSEL
     ECTWAGIRPQ TGDGLPYLGE HPKYRGLFIA AGHFRNGILL SPITGELAAQ WADGQAVPEL
     EPFRVDRSFP SFIT
//
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