ID   CP450_HELAN             Reviewed;         155 AA.
AC   P85191;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Cytochrome P450 {ECO:0000250|UniProtKB:O81117};
DE            EC=1.14.-.-;
DE   Flags: Fragment;
OS   Helianthus annuus (Common sunflower).
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=4232;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. RHA801 {ECO:0000269|Ref.1};
RA   Kozik A., Michelmore R.W., Knapp S., Matvienko M., Rieseberg L., Lin H.,
RA   van Damme M., Lavelle D., Chevalier P., Ziegle J., Ellison P., Kolkman J.,
RA   Slabaugh M.S., Livingston K., Zhou Y., Lai Z., Church S., Jackson L.,
RA   Bradford K.;
RT   "Lettuce and sunflower ESTs from the compositae genome project
RT   http://compgenomics.ucdavis.edu/.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RA   Garcia J.S., Souza G.H.M.F., Eberlin M.N., Arruda M.A.Z.;
RT   "Evaluation of metal-ion stress in sunflower (Heliantus annus L.) leaves
RT   through proteomic changes.";
RL   Metallomics 1:107-113(2009).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:O81117};
CC   -!- INDUCTION: Down-regulated in response to mixed metal ion contamination
CC       (cadmium, copper, lead and zinc), but not in response to zinc ion
CC       contamination. {ECO:0000269|Ref.2}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000255}.
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DR   EMBL; BQ968925; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P85191; -.
DR   SMR; P85191; -.
DR   EnsemblPlants; mRNA:HanXRQr2_Chr13g0581001; CDS:HanXRQr2_Chr13g0581001.1; HanXRQr2_Chr13g0581001.
DR   Gramene; mRNA:HanXRQr2_Chr13g0581001; CDS:HanXRQr2_Chr13g0581001.1; HanXRQr2_Chr13g0581001.
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; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   SUPFAM; SSF48264; SSF48264; 1.
PE   1: Evidence at protein level;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           <1..155
FT                   /note="Cytochrome P450"
FT                   /id="PRO_0000397224"
FT   BINDING         99
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|UniProtKB:O81117"
FT   NON_TER         1
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   155 AA;  17774 MW;  B239B2336F80F537 CRC64;
     LGELKHLHYL HAALHESMRL YPPVQFDSKF AKHDDVLPDG TFVKRGSRVT YHPYAMGRME
     RIWGADSLEF KPERWIRDGE FKQERAYKYP VYQGGVRVCL GKEMSLVEMA SVALCLIRRF
     DVSVVNHSQL RFAPGLTATV SGGVHATVRR RDLSQ