ID   B3R862_CUPTR            Unreviewed;       531 AA.
AC   B3R862;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=FAD flavoprotein oxidoreductase, GMC family Oxidoreductase {ECO:0000313|EMBL:CAQ71112.1};
GN   OrderedLocusNames=RALTA_A3195 {ECO:0000313|EMBL:CAQ71112.1};
OS   Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS   107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=977880 {ECO:0000313|EMBL:CAQ71112.1, ECO:0000313|Proteomes:UP000001692};
RN   [1] {ECO:0000313|EMBL:CAQ71112.1, ECO:0000313|Proteomes:UP000001692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 /
RC   R1 {ECO:0000313|Proteomes:UP000001692};
RX   PubMed=18490699; DOI=10.1101/gr.076448.108;
RA   Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA   Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA   Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA   Masson-Boivin C.;
RT   "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT   comparative genomics of rhizobia.";
RL   Genome Res. 18:1472-1483(2008).
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; CU633749; CAQ71112.1; -; Genomic_DNA.
DR   RefSeq; WP_012354377.1; NC_010528.1.
DR   AlphaFoldDB; B3R862; -.
DR   GeneID; 29762586; -.
DR   KEGG; cti:RALTA_A3195; -.
DR   eggNOG; COG2303; Bacteria.
DR   HOGENOM; CLU_008878_3_0_4; -.
DR   BioCyc; CTAI977880:RALTA_RS15620-MONOMER; -.
DR   Proteomes; UP000001692; Chromosome 1.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   PANTHER; PTHR46056:SF4; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
FT   DOMAIN          79..298
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          384..519
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   531 AA;  56828 MW;  8E0DF573307F06A0 CRC64;
     MAIDNLYDAG IAAGWKVLDA STFTTTRTLD ADVVIVGSGA GGGISAEALS RAGLRVVLLE
     EGALRTSDSF RDMDENRAYR ELYQEAAART TADGAIAILQ GRAVGGSTTV NWSSSFRTPP
     QTLAHWATHH AVTGHGEAEM APWFDQVEAR LGIAPWAMAP NPNNDVLRRG CETLGWEWHV
     IPRNVKGCWN SGYCGFGCPV NAKQSMLVST IPAALASGAT LVHRVRVRTL DHDGQRVRSV
     TGEALGADGY TPTGIAVVVR ARHVVAAGGA INTPALLLRS RVPDPHQRLG LRTFIHPVNI
     SIAKMPERID PYYGAPQSIA SDHFQWQHGA TGPMGYKLEV PPMFPGISAG VVNGVGDALR
     RDMAQLPNTN AMLALLRDGF VPDSPGGRVR LAPDGSPLLD YEMTDYAWDG VRRAWLSMAQ
     AQFAAGAERV RPAHLDAAEY RSWPEARDAI ARLPLKPFRT ALFTAHLMGG CGMSDDPRGG
     VVDSRGRHHQ LANLSVFDGS VFPTSVGANP QLSVFALSAQ NADALARNLT S
//