ID   C76B7_ARNEU             Reviewed;         496 AA.
AC   A0A3Q9R4N5;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   10-APR-2019, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Geranylhydroquinone 3''-hydroxylase CYP76B74 {ECO:0000305};
DE            EC=1.14.14.174 {ECO:0000269|PubMed:30498024};
DE   AltName: Full=Cytochrome P450 76B74 {ECO:0000303|PubMed:30498024};
GN   Name=CYP76B74 {ECO:0000303|PubMed:30498024};
OS   Arnebia euchroma (Pink arnebia) (Lithospermum euchromon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Boraginales; Boraginaceae; Boraginoideae; Lithospermeae;
OC   Arnebia.
OX   NCBI_TaxID=373122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=30498024; DOI=10.1104/pp.18.01056;
RA   Wang S., Wang R., Liu T., Lv C., Liang J., Kang C., Zhou L., Guo J.,
RA   Cui G., Zhang Y., Werck-Reichhart D., Guo L., Huang L.;
RT   "CYP76B74 catalyzes the 3''-hydroxylation of geranylhydroquinone in
RT   shikonin biosynthesis.";
RL   Plant Physiol. 179:402-414(2019).
CC   -!- FUNCTION: Hydroxylase involved in the biosynthesis pathway of the red
CC       naphthoquinone pigment shikonin (PubMed:30498024). Catalyzes the key
CC       step C-3''-hydroxylation of the prenylated phenolic intermediate
CC       geranylhydroquinone to form 3''-hydroxygeranylhydroquinone
CC       (PubMed:30498024). {ECO:0000269|PubMed:30498024}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=geranylhydroquinone + O2 + reduced [NADPH--hemoprotein
CC         reductase] = 3''-hydroxygeranylhydroquinone + H(+) + H2O + oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:28146, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:24233,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:61158;
CC         EC=1.14.14.174; Evidence={ECO:0000269|PubMed:30498024};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28147;
CC         Evidence={ECO:0000269|PubMed:30498024};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:Q96242};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:30498024}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; MH077962; AZU97066.1; -; mRNA.
DR   KEGG; ag:AZU97066; -.
DR   BRENDA; 1.14.14.174; 13261.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 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   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..496
FT                   /note="Geranylhydroquinone 3''-hydroxylase CYP76B74"
FT                   /id="PRO_0000455169"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         436
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:Q96242"
SQ   SEQUENCE   496 AA;  55741 MW;  8983686FD1A55258 CRC64;
     MEYTTILVGF LIGFVLFKAL TRKSKNLPPG PHVLPIIGNL HLVGSIPHKS ILKLAEKYGP
     IMSLQFGQIP TIVVSSPSMA KEILQKQDVA FAGKRIPDAL NAHNHWQFSV VWLPANSLWR
     TLRKILTSNI FTNNRLEASQ HLRSQKVRDL VEYCKKSGDK GEAVEIGQAA YRTSLNLLSS
     TIFSKDLADY YSETGAPREF KDAIWNILVE SVKPNLADFV PILSMFDLQG IKRRAGIHFG
     KGLKIMEGLV NERLEHRETH GATHNDILDI FLNYCDEHPD ELDRHRVKHT ILDLFIAGTD
     TTSSVTEWTM AELIQNPQVM KRAKDELAQV IGKGKCLEES DVARLPYLRC IMKEALRKHP
     PGPFLFPRRP EEDVEVAGYT IPKGAQVLVS IYALGRDPNS WEDPLAFKPE RFLDSELDFR
     GNNFEMLPFG AGRRSCPGLP MAVRMVPLLL GSLINSFDWV LDGGMKPEDL SMEEKVGLTA
     QLAHPLKIVP IPVKEE