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
//