ID F6FWU7_ISOV2 Unreviewed; 389 AA.
AC F6FWU7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Glycine oxidase ThiO {ECO:0000313|EMBL:AEG43519.1};
GN OrderedLocusNames=Isova_0733 {ECO:0000313|EMBL:AEG43519.1};
OS Isoptericola variabilis (strain 225).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Isoptericola.
OX NCBI_TaxID=743718 {ECO:0000313|Proteomes:UP000009236};
RN [1] {ECO:0000313|EMBL:AEG43519.1, ECO:0000313|Proteomes:UP000009236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=225 {ECO:0000313|Proteomes:UP000009236};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Zeytun A., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Siebers A., Allgaier M., Thelen M.,
RA Hugenholtz P., Gladden J., Woyke T.;
RT "Complete sequence of Isoptericola variabilis 225.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004948}.
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DR EMBL; CP002810; AEG43519.1; -; Genomic_DNA.
DR AlphaFoldDB; F6FWU7; -.
DR STRING; 743718.Isova_0733; -.
DR KEGG; iva:Isova_0733; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_4_5_11; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000009236; 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:UP000009236}.
FT DOMAIN 2..361
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT REGION 251..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 389 AA; 39637 MW; 02846AC451895055 CRC64;
MVVVGAGIVG AAVAWRAARA GLRVTVLDPS PGDGATRAAA GMLAPVSETW FGEQAAVRLG
LAGRDAWPAF AAELAAETGA DPGLRPTGTL LVAYDADDAA HLRRWLDLHA SWSLESAALA
PAEARRREPL LGPRLAGAAW VPGDDVADPR ATHAALLAAL RERRGAAVVP RAGVRLLRDA
RGAVVGVVDD AGETHRAGAV VLATGWRAAE LVAGLPVAVP VRPVRGQTLR LDAGPDVAPS
HVVRGTVQGR PVYVVPRGPG TGRGPGATPE HREVVVGATS EEGPDDRRAT AGGVFALLRD
ARALLPGLDE AALVETTARA RPATPDNLPL VGPTDVPGLH LAAGHHRNGV LLAPVTADAV
VAGLEGDDPP AALAAADPRR FTPTPVRGA
//
