ID C5AT63_METEA Unreviewed; 411 AA.
AC C5AT63;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Glycine oxidase {ECO:0000313|EMBL:ACS38373.1};
DE EC=1.4.3.19 {ECO:0000313|EMBL:ACS38373.1};
GN Name=thiO {ECO:0000313|EMBL:ACS38373.1};
GN OrderedLocusNames=MexAM1_META1p0430 {ECO:0000313|EMBL:ACS38373.1};
OS Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS 9133 / AM1) (Methylobacterium extorquens).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=272630 {ECO:0000313|EMBL:ACS38373.1, ECO:0000313|Proteomes:UP000009081};
RN [1] {ECO:0000313|EMBL:ACS38373.1, ECO:0000313|Proteomes:UP000009081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
RC {ECO:0000313|Proteomes:UP000009081};
RX PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA Lidstrom M.E.;
RT "Methylobacterium genome sequences: a reference blueprint to investigate
RT microbial metabolism of C1 compounds from natural and industrial sources.";
RL PLoS ONE 4:E5584-E5584(2009).
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004948}.
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DR EMBL; CP001510; ACS38373.1; -; Genomic_DNA.
DR RefSeq; WP_012752103.1; NC_012808.1.
DR AlphaFoldDB; C5AT63; -.
DR STRING; 272630.MexAM1_META1p0430; -.
DR KEGG; mea:Mex_1p0430; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_4_5_5; -.
DR OrthoDB; 9790035at2; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000009081; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0043799; F:glycine oxidase activity; IEA:UniProtKB-EC.
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 Oxidoreductase {ECO:0000313|EMBL:ACS38373.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009081}.
FT DOMAIN 29..380
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 411 AA; 43072 MW; C3AD7901B30DCE0C CRC64;
MSDLLTSPIG QRRSLTIRPR AAELPQRADV AVVGAGLIGL SIAWQLAQAG RSVAVVERGN
VGSGASLAAT GMLAPAAEHE PGSDLLLPLA LESLRRWPAF RDALQAASGR EIDYRTDGTL
VIAIGRDEVE RLRFRHDLQR RSGVAAEWLS GPEVRAREPL LRPNVTAGIL CPLDAQVDPR
LVMEALLRAC EAAGVVISEG VAVEGLERRG GRVTGLHAAG RTLAADTVIL AAGAWSGDAS
LLPSDLDVPD LSVPVRPLKG QSLALRTTKR TGTLSRMVWT DAVHMAPKGD GHLIVGATVE
DCGFTSGVTA GGMFALLEGA RRVLPGIEEM EIDAVWSGFR PTSDDDAPII EEAAPGLVLA
TGHHRNGYLL APATADAVAT LLTEGALPDF ARGFGRARFA SSYQTGGRAV A
//
