ID   KAO1_HORVU              Reviewed;         499 AA.
AC   Q9AXH9;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Ent-kaurenoic acid oxidase 1;
DE            EC=1.14.14.107 {ECO:0000269|PubMed:11172076};
DE   AltName: Full=gpr5;
GN   Name=KAO1; Synonyms=GPR5;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND MUTANT M594.
RC   STRAIN=cv. Himalaya;
RX   PubMed=11172076; DOI=10.1073/pnas.98.4.2065;
RA   Helliwell C.A., Chandler P.M., Poole A., Dennis E.S., Peacock J.W.;
RT   "The CYP88A cytochrome P450, ent-kaurenoic acid oxidase, catalyzes three
RT   steps of the gibberellin biosynthesis pathway.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:2065-2070(2001).
CC   -!- FUNCTION: Catalyzes three successive oxidations of ent-kaurenoic acid
CC       giving gibberellin 12 (GA12), a key step in gibberellins (GAs)
CC       biosynthesis. GAs, which are involved many processes, including stem
CC       elongation, play a central role in plant development.
CC       {ECO:0000269|PubMed:11172076}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ent-kaur-16-en-19-oate + 3 O2 + 3 reduced [NADPH--hemoprotein
CC         reductase] = gibberellin A12 + 4 H(+) + 4 H2O + 3 oxidized [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:33219, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57297, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:58627; EC=1.14.14.107;
CC         Evidence={ECO:0000269|PubMed:11172076};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
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; AF326277; AAK11616.1; -; mRNA.
DR   AlphaFoldDB; Q9AXH9; -.
DR   SMR; Q9AXH9; -.
DR   EnsemblPlants; HORVU.MOREX.r2.7HG0529910.1; HORVU.MOREX.r2.7HG0529910.1; HORVU.MOREX.r2.7HG0529910.
DR   EnsemblPlants; HORVU.MOREX.r2.7HG0529910.1.mrna1; HORVU.MOREX.r2.7HG0529910.1.mrna1; HORVU.MOREX.r2.7HG0529910.1.
DR   Gramene; HORVU.MOREX.r2.7HG0529910.1; HORVU.MOREX.r2.7HG0529910.1; HORVU.MOREX.r2.7HG0529910.
DR   Gramene; HORVU.MOREX.r2.7HG0529910.1.mrna1; HORVU.MOREX.r2.7HG0529910.1.mrna1; HORVU.MOREX.r2.7HG0529910.1.
DR   OMA; EMGWPMV; -.
DR   BRENDA; 1.14.13.79; 2687.
DR   BRENDA; 1.14.14.107; 2687.
DR   UniPathway; UPA00390; -.
DR   ExpressionAtlas; Q9AXH9; baseline and differential.
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   GO; GO:0009686; P:gibberellin biosynthetic process; IEA:UniProtKB-UniPathway.
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..499
FT                   /note="Ent-kaurenoic acid oxidase 1"
FT                   /id="PRO_0000052180"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         443
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   MUTAGEN         372
FT                   /note="N->K: In M594; induces dwarfism, due to accumulation
FT                   of kaurenoic acid."
SQ   SEQUENCE   499 AA;  55876 MW;  76CB0C5CC6C3641F CRC64;
     MGEGAWWAVA AVVAALAVVA LDAAVRAAHA WYWTASLGAG RRGRLPPGDM GWPLVGGMWA
     FLRAFKSGRP DSFIDSFARR FGRAGLYRAF MFSSPTIMAT TPEACKQVLM DDDAFVTGWP
     KATVALIGPK SFVNMGYDEH RRLRKLTAAP INGFDALTSY LGFIDDTVVT TLRGWSERGG
     DGHFEFLTEL RRMTFRIIVQ IFMGGADERT AAELERTYTE LNYGMRAMAI DLPGFAYHKA
     IRARRRLVAA LQRVLDERRA RGGKTAAGAA APVDMMDRLI AVEDEGGRRL QDDEIIDVLV
     MYLNAGHESS GHITMWATVF LQENPEILAK AKAEQEAIMR SIPPGQKGLT LRDFRKMAYL
     SQVVDETLRF VNISFVSFRQ ATRDVFVNGY LIPKGWKVQL WYRSVHMDPQ VYPDPKKFDP
     SRWEGPPPRA GTFLPFGLGT RLCPGNDLAK LEISVFLHHF LLGYKLTRKN PNCRVRYLPH
     PRPVDNCLAK ITRLSSSHG