ID D6ZFI1_SEGRD Unreviewed; 374 AA.
AC D6ZFI1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Glycine oxidase ThiO {ECO:0000313|EMBL:ADG97705.1};
GN OrderedLocusNames=Srot_1235 {ECO:0000313|EMBL:ADG97705.1};
OS Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM
OS 44985 / JCM 13578).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Segniliparaceae;
OC Segniliparus.
OX NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG97705.1, ECO:0000313|Proteomes:UP000002247};
RN [1] {ECO:0000313|EMBL:ADG97705.1, ECO:0000313|Proteomes:UP000002247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC {ECO:0000313|Proteomes:UP000002247};
RX PubMed=21304703; DOI=10.4056/sigs.791633;
RA Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M., Schneider S.,
RA Bruce D., Goodwin L., Pitluck S., Liolios K., Mikhailova N., Pati A.,
RA Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chertkov O., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Detter J.C., Han C.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT 1076).";
RL Stand. Genomic Sci. 2:203-211(2010).
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004948}.
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DR EMBL; CP001958; ADG97705.1; -; Genomic_DNA.
DR RefSeq; WP_013138161.1; NC_014168.1.
DR AlphaFoldDB; D6ZFI1; -.
DR STRING; 640132.Srot_1235; -.
DR KEGG; srt:Srot_1235; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_4_5_11; -.
DR OrthoDB; 3214401at2; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000002247; 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; SSF51971; Nucleotide-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002247}.
FT DOMAIN 7..348
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 374 AA; 38378 MW; 0E3E6F295A8EEA15 CRC64;
MTRSLDILGA GVIGLSIAWR AAQRGRSVRV WDRSVGAPSQ PGASASWVAG GMLAPFSEAW
PGHEPLLRLG ADSLARWPAF AAELGANSPD GTVLAAQGTL VVGATAADLA ALAPGLESAR
GAGLDSRRSA RAELREIEPG LAADVRGGWI LPQEPAADNR ALLAALAAAA RGAGVEFVAQ
SPAQLPDSGA DDLVVAVGAA APALLPGLPV RPVKGEILRL AASSRTAPPP KRTIRALVRG
RHVYLVPRRD GVVVGATELE GDARAGVSAQ AIVELLSDAL AILPGLADYE LVEACAGFRP
VTPDRCPLLG WTSRPATGPR SAGRCLVATG HGRDGMLLAP LTADLAVALL DNEQVSEQDQ
EALRAMDPAR FPYG
//
