ID   CPXX_RHORH              Reviewed;          20 AA.
AC   P31718;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Cytochrome P450-RR1;
DE            Short=Cytochrome P450RR1;
DE            EC=1.14.-.-;
DE   AltName: Full=Cytochrome P450-RRI;
DE   Flags: Fragment;
OS   Rhodococcus rhodochrous.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=1829;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=116;
RX   PubMed=8477696; DOI=10.1111/j.1432-1033.1993.tb17750.x;
RA   Eltis L.D., Karlson U., Timmis K.N.;
RT   "Purification and characterization of cytochrome P450RR1 from Rhodococcus
RT   rhodochrous.";
RL   Eur. J. Biochem. 213:211-216(1993).
CC   -!- FUNCTION: P450-RRI catalyzes the O-dealkylation of 2-ethoxyphenol and
CC       2-methoxyphenol to produce catechol. The cytochrome binds other ortho-
CC       substituted phenols, including 2-ethoxyphenol, 2-methylphenol and 2-
CC       chlorophenol.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- INDUCTION: By 2-ethoxyphenol.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   AlphaFoldDB; P31718; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Heme; Iron; Metal-binding; Monooxygenase;
KW   Oxidoreductase.
FT   CHAIN           1..>20
FT                   /note="Cytochrome P450-RR1"
FT                   /id="PRO_0000052232"
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2428 MW;  BCA81586D8DD1496 CRC64;
     TSTLSWLDEI TMEELERNPY