ID   C1B1U3_RHOOB            Unreviewed;       533 AA.
AC   C1B1U3;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=Putative L-sorbose dehydrogenase {ECO:0000313|EMBL:BAH50367.1};
DE            EC=1.1.99.32 {ECO:0000313|EMBL:BAH50367.1};
GN   OrderedLocusNames=ROP_21200 {ECO:0000313|EMBL:BAH50367.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH50367.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH50367.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH50367.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; AP011115; BAH50367.1; -; Genomic_DNA.
DR   RefSeq; WP_012689323.1; NC_012522.1.
DR   AlphaFoldDB; C1B1U3; -.
DR   STRING; 632772.ROP_21200; -.
DR   KEGG; rop:ROP_21200; -.
DR   PATRIC; fig|632772.20.peg.2215; -.
DR   HOGENOM; CLU_002865_7_1_11; -.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000002212; Chromosome.
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; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968};
KW   Oxidoreductase {ECO:0000313|EMBL:BAH50367.1}.
FT   DOMAIN          81..104
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          254..268
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         83
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         91..94
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         219
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   533 AA;  57073 MW;  047C61F1392DA2B5 CRC64;
     MSATYDYVIA GGGTAGCVLA GRLTEDPNVR VLLLEAGGND RHPFIHVPAG FAKLTASKYD
     WGFSSVPQKH CNDRVIPLAQ GKVIGGGGSI NAQVFTRGAH EDYDEWALKY GCAGWSFDEI
     QKYFLRSEDN ERLSAPYHGT DGPLGVSDPI NPHPLSKSFV QAGQEFGLPF NGDFNGDRQH
     GVGLYQTTTK NARRCSAAGA YLAPARKRPN LTVRENVAVS RVLLDGGRAT GIEVLTPHGV
     ETFRASREVL VAAGAFGSPK ILQLSGIGHP DDLRDANVEV AHALPGVGRN LHDHCDLDVI
     YELREYQSLD RLNLIRPATA KAGLEYAAFR RGPLASTVVE AGGFSFGHAG ESIPDLQFHF
     LPAAGVEAGV AAVRPGYGCT LNSYALRPES RGSVKIRSND PTAAPLIDPN FLATDFDLES
     SIEGLRQSRE IMAQSSMARH IKAEHLAGGL SVNTKDDYVK FVRAYGRTSY HPVGTCAMGV
     GDEAVVSPEL KVQGIEGLRV VDSSVMPRIV SSNTQAPTVM IAEKAVDLIR GEG
//