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Database: UniProt
Entry: Q0SFJ8_RHOJR
LinkDB: Q0SFJ8_RHOJR
Original site: Q0SFJ8_RHOJR 
ID   Q0SFJ8_RHOJR            Unreviewed;       518 AA.
AC   Q0SFJ8;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 121.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:ABG93688.1};
DE            EC=1.1.99.1 {ECO:0000313|EMBL:ABG93688.1};
GN   OrderedLocusNames=RHA1_ro01877 {ECO:0000313|EMBL:ABG93688.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG93688.1, ECO:0000313|Proteomes:UP000008710};
RN   [1] {ECO:0000313|Proteomes:UP000008710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; CP000431; ABG93688.1; -; Genomic_DNA.
DR   RefSeq; WP_011594794.1; NC_008268.1.
DR   AlphaFoldDB; Q0SFJ8; -.
DR   KEGG; rha:RHA1_ro01877; -.
DR   PATRIC; fig|101510.16.peg.1898; -.
DR   eggNOG; COG2303; Bacteria.
DR   HOGENOM; CLU_002865_7_1_11; -.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0008812; F:choline dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   Gene3D; 3.30.410.40; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11552:SF152; OXIDASE (CODA), PUTATIVE (AFU_ORTHOLOGUE AFUA_8G04090)-RELATED; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 2.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Oxidoreductase {ECO:0000313|EMBL:ABG93688.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT   DOMAIN          259..273
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         84
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         221
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   518 AA;  56550 MW;  0E20CBC0B6FF3E5B CRC64;
     MTDTVFDYVI AGGGTAGCVL AARLSEDPSV TVCLVEAGPS DVGDRNVLEL SQWMHLLDSG
     YDWDYPVEPQ EKGNSFMRHA RAKVLGGCSS HNSCIAFWPP AETLDDWAAA GATGWGAKDV
     LPLVARVENN DAPGEQHGRS GPVRLRDVPP HDPCGVALLE AAAKVGLPTV QFNRGTTVLD
     GAGWFQINAS EDGTRMSTSH AYLHPILGSR PNLEVRTDCR VSEIVIDDAL AATGVRYQRP
     DLTGYDTVSA RREVIVTAGA IDTPKLLMLS GIGPTVHLRE MGVQVRVDAP GVGQNLDDHV
     EGLVFWDASR PMVETSTQWW EIGLFATTEE GLNHPDLMMH YGSVPFDMNT LRWGYPTTDN
     GFCLTPNVTQ GLSRGTVRLR SRDFRDRPRV DPRYFTDPDG HDEAVMLAGI RLARRIAEQE
     PLRGWITREL APGPEAVTDD ELIDYAHRTH NTVYHPAGTA RMGAATDPMA VLDPELRVKG
     VRDLRVVDAS AMPKLPYVNP NITVMTMAEK CADLIRGT
//
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