YTH2_RHOER
ID YTH2_RHOER Reviewed; 493 AA.
AC P46371;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Uncharacterized GMC-type oxidoreductase in thcA 5'region;
DE EC=1.1.-.-;
DE AltName: Full=ORF2;
OS Rhodococcus erythropolis (Arthrobacter picolinophilus).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC Rhodococcus erythropolis group.
OX NCBI_TaxID=1833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NI86/21;
RX PubMed=7836301; DOI=10.1128/jb.177.3.676-687.1995;
RA Nagy I., Schoofs G., Compernolle F., Proost P., Vanderleyden J., de Mot R.;
RT "Degradation of the thiocarbamate herbicide EPTC (S-ethyl
RT dipropylcarbamothioate) and biosafening by Rhodococcus sp. strain NI86/21
RT involve an inducible cytochrome P-450 system and aldehyde dehydrogenase.";
RL J. Bacteriol. 177:676-687(1995).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; U17129; AAC77470.1; -; Genomic_DNA.
DR AlphaFoldDB; P46371; -.
DR SMR; P46371; -.
DR STRING; 1833.XU06_08910; -.
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; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023978; GMC_oxidoreductase_actinobac.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; PTHR11552; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR03970; Rv0697; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Oxidoreductase.
FT CHAIN 1..493
FT /note="Uncharacterized GMC-type oxidoreductase in thcA
FT 5'region"
FT /id="PRO_0000205619"
FT ACT_SITE 429
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 8..37
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 493 AA; 53022 MW; 8E00EC6BFE552D71 CRC64;
MTEADYADFL VVGGGTCGCV VAARLSEDPS ATVMLLESGS GYRSALELPD VLGDPYRLPV
GPASEYTWTY PVELTPRRAS TIARGRTLGG SGAVNGAYFM RATRADFENW PSAWRYDDVL
PYFKKSETDR DFESEFHGTA GPIPVERRAW DQLHPLSGEF HAAALGAGFP DDVDKNAPDS
FGVGRVPLNV ADHRRISTAI GYLMPALHRP NLRVESGVNV IRIVFSGTRA VGVDVLDDGN
VRRIHADHVI VCSGAVATPH ILLNSGVGPA EQLAEQGVSV ILDRHGVGQN FVDHPEVLLP
YHFSTPRAIR SQTPVLETAL NLAELEIRPY TASFTDLVPG VPRMDHGVGV VLMAPRSRGS
IELASGDPAG APRIRYNYVA STHDRAANRE GMQIAENLLE SIAETGLIDR PVVEYTDEWV
ESRLGTSLHM SGSCVMGAES DPFAVVDDRC RVIGAQGLSI VDTSILPTIP TRGPHATAVM
VAERASAILL GDE