ID   C76B1_HELTU             Reviewed;         490 AA.
AC   O23976; O48603;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=7-ethoxycoumarin O-deethylase;
DE            Short=ECOD;
DE            EC=1.14.-.-;
DE   AltName: Full=Cytochrome P450 76B1;
DE   AltName: Full=Phenylurea dealkylase;
GN   Name=CYP76B1;
OS   Helianthus tuberosus (Jerusalem artichoke) (Helianthus tomentosus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Heliantheae; Helianthus.
OX   NCBI_TaxID=4233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Blanc commun; TISSUE=Tuber;
RX   PubMed=9681028; DOI=10.1046/j.1365-313x.1998.00099.x;
RA   Batard Y., Leret M., Schalk M., Zimmerlin A., Durst F., Werck-Reichhart D.;
RT   "Molecular cloning and functional expression in yeast of CYP76B1, a
RT   xenobiotic-inducible 7-ethoxycoumarin O-deethylase from Helianthus
RT   tuberosus.";
RL   Plant J. 14:111-120(1998).
RN   [2]
RP   CHARACTERIZATION.
RC   STRAIN=cv. Blanc commun; TISSUE=Tuber;
RX   PubMed=9808750; DOI=10.1104/pp.118.3.1049;
RA   Robineau T., Batard Y., Nedelkina S., Cabello-Hurtado F., Leret M.,
RA   Sorokine O., Didierjean L., Werck-Reichhart D.;
RT   "The chemically inducible plant cytochrome P450 CYP76B1 actively
RT   metabolizes phenylureas and other xenobiotics.";
RL   Plant Physiol. 118:1049-1056(1998).
CC   -!- FUNCTION: Capable of dealkylating a model xenobiotic compound, 7-
CC       ethoxycoumarin. Metabolizes with high efficiency a wide range of
CC       xenobiotics, including alkoxycoumarins, alkoxyresorufins, and several
CC       herbicides of the class of phenylureas. Catalyzes the double N-
CC       dealkylation (oxidative N-demethylation) of phenylureas such as
CC       chlortoluron and isoproturon with turnover rates comparable to those
CC       reported for physiological substrates and produces non-phytotoxic
CC       compounds. Could be used for control of herbicide tolerance and
CC       selectivity, as well as soil and groundwater bioremediation.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- INDUCTION: By aminopyrine and other xenobiotics.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Y09920; CAA71054.1; -; mRNA.
DR   EMBL; Y10098; CAA71178.1; -; mRNA.
DR   PIR; T10773; T10773.
DR   PIR; T10895; T10895.
DR   AlphaFoldDB; O23976; -.
DR   SMR; O23976; -.
DR   KEGG; ag:CAA71054; -.
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   GO; GO:0051762; P:sesquiterpene biosynthetic process; IEA:UniProt.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..490
FT                   /note="7-ethoxycoumarin O-deethylase"
FT                   /id="PRO_0000052140"
FT   BINDING         432
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"
FT   CONFLICT        16..17
FT                   /note="LI -> HE (in Ref. 1; CAA71178)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        194
FT                   /note="D -> DSA (in Ref. 1; CAA71178)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        224
FT                   /note="K -> R (in Ref. 1; CAA71178)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   490 AA;  54991 MW;  E3E77B7B7905C1CF CRC64;
     MDFLIIVSTL LLSYILIWVL GVGKPKNLPP GPTRLPIIGN LHLLGALPHQ SLAKLAKIHG
     PIMSLQLGQI TTLVISSATA AEEVLKKQDL AFSTRNVPDA VRAYNHERHS ISFLHVCTEW
     RTLRRIVSSN IFSNSSLEAK QHLRSKKVEE LIAYCRKAAL SNENVHIGRA AFRTSLNLLS
     NTIFSKDLTD PYEDSGKEFR EVITNIMVDS AKTNLVDVFP VLKKIDPQGI KRGMARHFSK
     VLGIFDQLIE ERMRTGRFEQ GDVLDVCLKM MQDNPNEFNH TNIKALFLDL FVAGTDTTSI
     TIEWAMTELL RKPHIMSKAK EELEKVIGKG SIVKEDDVLR LPYLSCIVKE VLRLHPPSPL
     LLPRKVVTQV ELSGYTIPAG TLVFVNAWAI GRDPTVWDDS LEFKPQRFLE SRLDVRGHDF
     DLIPFGAGRR ICPGIPLATR MVPIMLGSLL NNFDWKIDTK VPYDVLDMTE KNGTTISKAK
     PLCVVPIPLN