ID   THCD_RHOER              Reviewed;         427 AA.
AC   P43494;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Rhodocoxin reductase;
DE            EC=1.18.1.-;
GN   Name=thcD;
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], AND PROTEIN SEQUENCE OF 2-11.
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   -!- FUNCTION: The degradation of the thiocarbamate herbicide EPTC by
CC       cytochrome CYP116 (thcB) requires the participation of a flavoprotein,
CC       rhodocoxin reductase, and an iron-sulfur protein, rhodocoxin, to
CC       mediate the transfer of electrons from NADH to P450 for oxygen
CC       activation.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; U17130; AAC45752.1; -; Genomic_DNA.
DR   AlphaFoldDB; P43494; -.
DR   SMR; P43494; -.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR028202; Reductase_C.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF14759; Reductase_C; 1.
DR   SUPFAM; SSF51905; SSF51905; 2.
DR   SUPFAM; SSF55424; SSF55424; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; FAD; Flavoprotein; NAD; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7836301"
FT   CHAIN           2..427
FT                   /note="Rhodocoxin reductase"
FT                   /id="PRO_0000167647"
FT   BINDING         2..34
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   BINDING         144..172
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   427 AA;  45270 MW;  089253050B7A1F92 CRC64;
     MSIVIIGSGQ AGFEAAVSLR SHGFSGTITL VGDEPGVPYQ RPPLSKAYLH SDPDRESLAL
     RPAQYFDDHR ITLTCGKPVV RIDRDAQRVE LIDATAIEYD HLILATGARN RLLPVPGANL
     PGVHYLRTAG EAESLTSSMA SCSSLVVIGA GFIGLEVAAA ARKKGLDVTV VEAMDRPMAR
     ALSSVMSGYF STAHTEHGVH MRLSTGVKTI NAADGRAAGV TTNSGDVIHA DAVVVGIGVV
     PNIELAALTG LPVDNGIVVD EYLRTPDENI SAIGDCAAYP IPGKAGLVRL ESVQNAVDQA
     RCLAAQLTGT STHYRSVPWF WSEQYESKLQ MAGLTAGADT HVVRGSVDSG VFSIFCFLGT
     RLLGVESVNK PRDHMAARKI LATEMPLTPE QAADTDFDLK LAIARHKDTH KDEVASADIG
     ERQVVAS