ID Q0RXH5_RHOJR Unreviewed; 505 AA.
AC Q0RXH5;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:ABH00011.1};
DE EC=1.1.-.- {ECO:0000313|EMBL:ABH00011.1};
GN OrderedLocusNames=RHA1_ro08967 {ECO:0000313|EMBL:ABH00011.1};
OS Rhodococcus jostii (strain RHA1).
OG Plasmid pRHL1 {ECO:0000313|EMBL:ABH00011.1,
OG ECO:0000313|Proteomes:UP000008710}.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABH00011.1, 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|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000432; ABH00011.1; -; Genomic_DNA.
DR RefSeq; WP_011599688.1; NC_008269.1.
DR AlphaFoldDB; Q0RXH5; -.
DR KEGG; rha:RHA1_ro08967; -.
DR PATRIC; fig|101510.16.peg.8253; -.
DR HOGENOM; CLU_002865_7_2_11; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000008710; Plasmid pRHL1.
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; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000313|EMBL:ABH00011.1};
KW Plasmid {ECO:0000313|EMBL:ABH00011.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT DOMAIN 252..266
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 82
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 90..93
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 217
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 505 AA; 54121 MW; 97A5ACD3F3F3D6D9 CRC64;
MKHFDYVIIG AGSAGCVMAD RLSNDERCTV LVLEAGPVDT DPRISDPARW VELGGSPVDW
GYLTEPQKYA AGRQIPWPRG RVVGGSSSIN AMVHMRGCAA DYDNWAAQGC TGWDYESVLP
TFKAYEDFDG GDSGYHGTRG PLKVSLPHDV HPLSEAALSA ALGLGHPANS DFNGETTLGV
GWNPLTVWDG RRQSAAVAFL GPALKRSNLT LRTGVLVTKL VSSQDRITGV EYVENGTART
VHVDGEVVLC AGAIETPKLL LLSGIGPTDD LKDLGITVTS HAPGVGANLH DHPGVGITFT
SKQPVVPGHN QHSELGMFAN IDGSPERPQV QFGVVLAPHV AEGLVAPPNG FTFYPSWTTP
ESRGSLKLRS ARPEDQPLID PCYLQTESDL DGLTGAIELS REWAHAPAME DWTDKEVLPG
PGIHDKQTLR DYVRRAVGTW FHPVGTCRMG SDIDSVVDNR LKLRAFDNAR VADASIIPTV
PLGNTNAPTL MIAHRAADFI LADAQ
//
