ID   THCB_RHOER              Reviewed;         437 AA.
AC   P43492;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Cytochrome P450 116;
DE            EC=1.14.-.-;
GN   Name=thcB; Synonyms=cyp116;
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 2-21.
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: Degradation of thiocarbamate herbicides.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- INDUCTION: By EPTC (S-ethyl dipropylcarbamothioate).
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; U17130; AAC45749.1; -; Genomic_DNA.
DR   AlphaFoldDB; P43492; -.
DR   SMR; P43492; -.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002397; Cyt_P450_B.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00359; BP450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Heme; Iron; Metal-binding; Monooxygenase;
KW   Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7836301"
FT   CHAIN           2..437
FT                   /note="Cytochrome P450 116"
FT                   /id="PRO_0000052230"
FT   BINDING         375
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   437 AA;  48927 MW;  D20099A9A8015EAA CRC64;
     MTVDHAPEGV KSPTGCPVSG MAADFDPFRG AYQVDPSSSL RQARKDEPVF FSPLLDYWVV
     TRYEDIKQIF KTPSVFSPSI TVDQITPISD EALQILGSYQ FAAGRMLVNE DEPIHTERRR
     LLMQPFEADN VATLEPKIRE VVNTYLDRVI KDGRADLIGD LLYEVPCIVA LIFLGVPDED
     IETCRQYGMQ QTLFTWGHPT GDEQTRVATG MGKFWEFAGG LVDKLKADPN AKGWIPHAIE
     MQRQHPDLFD DNYLQNIMFG GVFAAHETTT NATGNAFRTL LENRSSWDEI CADPTLIPKA
     IEECLRYSGS VVAWRRKAVV DTTVGEVDIP AGGRLLIVMA SANRDDSMFP EPDDFDIHRG
     NAQRHLTFGI GSHTCLGATL ARLEMKVFLE EVSRRLPHMS LVAGQEFSYL PNTSFRGPEH
     VLVEWDPQQN PVPADRP