ID   THCC_RHOER              Reviewed;         107 AA.
AC   P43493;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Rhodocoxin;
GN   Name=thcC;
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 2-8.
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: Ferredoxin-type protein which transfers electrons from
CC       rhodocoxin reductase to cytochrome CYP116 (ThcB), which is involved in
CC       the degradation of thiocarbamate herbicides.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family.
CC       {ECO:0000305}.
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DR   EMBL; U17130; AAC45751.1; -; Genomic_DNA.
DR   RefSeq; WP_015889129.1; NZ_JABBPH010000001.1.
DR   AlphaFoldDB; P43493; -.
DR   SMR; P43493; -.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0140647; P:P450-containing electron transport chain; IEA:InterPro.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR001055; Adrenodoxin.
DR   InterPro; IPR018298; Adrenodoxin_Fe-S_BS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   PANTHER; PTHR23426; PTHR23426; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   PRINTS; PR00355; ADRENODOXIN.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS00814; ADX; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7836301"
FT   CHAIN           2..107
FT                   /note="Rhodocoxin"
FT                   /id="PRO_0000201163"
FT   DOMAIN          2..106
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         40
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         46
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         49
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         87
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ   SEQUENCE   107 AA;  11546 MW;  6AC8C13CEF1A4DF8 CRC64;
     MPTVTYVHPD GTKHEVEVPT GKRVMQAAIG AGIDGIVAEC GGQAMCATCH VYVESPWADK
     FPSISEEEDE MLDDTVSPRT EASRLSCQLV VSDDVDGLIV RLPEEQV