ID A0A0A1MS80_9BACI Unreviewed; 378 AA.
AC A0A0A1MS80;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Glycine oxidase {ECO:0000313|EMBL:CEI81826.1};
GN Name=thiO {ECO:0000313|EMBL:CEI81826.1};
GN ORFNames=BN997_01680 {ECO:0000313|EMBL:CEI81826.1};
OS Oceanobacillus oncorhynchi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=545501 {ECO:0000313|EMBL:CEI81826.1, ECO:0000313|Proteomes:UP000040453};
RN [1] {ECO:0000313|EMBL:CEI81826.1, ECO:0000313|Proteomes:UP000040453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oc5 {ECO:0000313|EMBL:CEI81826.1,
RC ECO:0000313|Proteomes:UP000040453};
RA Urmite Genomes Urmite Genomes;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004948}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CDGG01000001; CEI81826.1; -; Genomic_DNA.
DR RefSeq; WP_042531224.1; NZ_JAUDBP010000005.1.
DR AlphaFoldDB; A0A0A1MS80; -.
DR STRING; 545501.BN997_01680; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000040453; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000040453}.
FT DOMAIN 8..348
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 378 AA; 41543 MW; 57994285F324F3B8 CRC64;
MNKQFDQIIV GGGVIGCSIA YQLAKRGNRV LVIERNQIGC EASSAAAGML GAQGEFTEDS
PLFRFAHESR ALFKNLSEEL KEASGVDIQY IHKGIMKLAF HQQQYSKLQS VASFQREAGN
PAYLLSVEEA KKMEPSLTEN LRAVLYLPDD GQVSARHLTK AFSLAASHYG AVLHEQESVN
ELLIENETVY GVRTTEAIYE AVQVIVATGA FGDELLPADY AAIPVKGECL LLELDQKLFQ
STLWMDGCYL VPKQGKKVIV GASSIPGKMD KHVHAASVQR LLSRAQKMVP ELAEARIRKM
WAGIRPSTAD ELPYLGEIPG IPGLYAAKGH YRNGILLSPI TGIYMADLIE NKPVSPLYYD
CFHADRQNKK LEKAGEST
//
