ID   Q0S7Z5_RHOJR            Unreviewed;       528 AA.
AC   Q0S7Z5;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   SubName: Full=Possible choline dehydrogenase {ECO:0000313|EMBL:ABG96341.1};
GN   OrderedLocusNames=RHA1_ro04555 {ECO:0000313|EMBL:ABG96341.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG96341.1, 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   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; CP000431; ABG96341.1; -; Genomic_DNA.
DR   RefSeq; WP_011596929.1; NC_008268.1.
DR   AlphaFoldDB; Q0S7Z5; -.
DR   KEGG; rha:RHA1_ro04555; -.
DR   PATRIC; fig|101510.16.peg.4591; -.
DR   eggNOG; COG2303; Bacteria.
DR   HOGENOM; CLU_008878_4_2_11; -.
DR   OrthoDB; 9798604at2; -.
DR   Proteomes; UP000008710; 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; 2.
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; 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   Pfam; PF13450; NAD_binding_8; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 2.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT   DOMAIN          91..310
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          393..504
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   528 AA;  57782 MW;  648C4B29271088D0 CRC64;
     MRDASVGEPT GPSKHSYDVV IVGSGMGGGT LAYALADSGV DVLLIERGDF LPQEKQNWDP
     QEVFEGHRYA NAEQWYDTEG RPFSPGTYYY VGGNTKLYGS SLARFRREDF QSTQHEAGES
     PEWPFSYDDF APYYARAEQV HRVHGDHTDD PTLPRDEPFP YPAIGHEPPV QEAADALRRL
     GYTPSNIPLG IDLRDGGGCI RCRTCDGFPC RVLAKSDADV CCVRPAIASG SVELLTNAYA
     ERVLTDETGH RATGVQIRHR GTELVVDART VVVSCGAVNS AALLLRSANA AHPDGLANSS
     GMVGRNYMVH NNSIMVGVNP LKKNTSEFQK TLYINDFYTH GTADHPYPLG HVQLIGKLQG
     EMIKGQRPLI PKWALSQATA RSMDWWLFTE DLPDPDNRVT LTDDGNIQIA WTPNNTRAHE
     VLVREVRKIL RKIGYPFVFS QGTGIEVNSH QAGTVRAGTD PATSVLDADC RAHDVGNLYV
     VDSSFFPSLP VMNPALSIAA NAFRVAESIA DRVGKTRSHD TPAQSASL
//