ID   C7019_ORYSJ             Reviewed;         503 AA.
AC   Q5Z5S6; A0A0P0WXZ0; Q68YV9;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Ent-kaurene oxidase-like 5 {ECO:0000303|PubMed:15316288};
DE            Short=OsKOL5 {ECO:0000303|PubMed:15316288};
DE            EC=1.14.13.- {ECO:0000305};
DE   AltName: Full=Cytochrome P450 701A9 {ECO:0000303|PubMed:22247270};
DE   AltName: Full=Ent-kaurene oxidase 5 {ECO:0000303|PubMed:15075394};
DE            Short=OsKO5 {ECO:0000303|PubMed:15075394};
DE   AltName: Full=OsKOS2 {ECO:0000303|PubMed:16299167};
GN   Name=CYP701A9 {ECO:0000303|PubMed:22247270};
GN   OrderedLocusNames=Os06g0568600 {ECO:0000312|EMBL:BAF19817.1},
GN   LOC_Os06g37224 {ECO:0000305};
GN   ORFNames=OSJNBa0062E01.13 {ECO:0000312|EMBL:BAD54586.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Xiushui 11;
RX   PubMed=16299167; DOI=10.1104/pp.105.072306;
RA   Zhu S., Gao F., Cao X., Chen M., Ye G., Wei C., Li Y.;
RT   "The rice dwarf virus P2 protein interacts with ent-kaurene oxidases in
RT   vivo, leading to reduced biosynthesis of gibberellins and rice dwarf
RT   symptoms.";
RL   Plant Physiol. 139:1935-1945(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   TISSUE SPECIFICITY, AND INDUCTION BY UV IRRADIATION.
RX   PubMed=15316288; DOI=10.1023/b:plan.0000038261.21060.47;
RA   Itoh H., Tatsumi T., Sakamoto T., Otomo K., Toyomasu T., Kitano H.,
RA   Ashikari M., Ichihara S., Matsuoka M.;
RT   "A rice semi-dwarf gene, Tan-Ginbozu (D35), encodes the gibberellin
RT   biosynthesis enzyme, ent-kaurene oxidase.";
RL   Plant Mol. Biol. 54:533-547(2004).
RN   [6]
RP   GENE FAMILY.
RX   PubMed=15075394; DOI=10.1104/pp.103.033696;
RA   Sakamoto T., Miura K., Itoh H., Tatsumi T., Ueguchi-Tanaka M., Ishiyama K.,
RA   Kobayashi M., Agrawal G.K., Takeda S., Abe K., Miyao A., Hirochika H.,
RA   Kitano H., Ashikari M., Matsuoka M.;
RT   "An overview of gibberellin metabolism enzyme genes and their related
RT   mutants in rice.";
RL   Plant Physiol. 134:1642-1653(2004).
RN   [7]
RP   FUNCTION.
RX   PubMed=22247270; DOI=10.1104/pp.111.187518;
RA   Wang Q., Hillwig M.L., Wu Y., Peters R.J.;
RT   "CYP701A8: a rice ent-kaurene oxidase paralog diverted to more specialized
RT   diterpenoid metabolism.";
RL   Plant Physiol. 158:1418-1425(2012).
CC   -!- FUNCTION: May hydroxylate diterpenes. {ECO:0000305|PubMed:22247270}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots. {ECO:0000269|PubMed:15316288}.
CC   -!- INDUCTION: By UV irradiation. {ECO:0000269|PubMed:15316288}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000255|RuleBase:RU000461}.
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DR   EMBL; AY660664; AAT81229.1; -; mRNA.
DR   EMBL; AP005471; BAD54586.1; -; Genomic_DNA.
DR   EMBL; AP008212; BAF19817.1; -; Genomic_DNA.
DR   EMBL; AP014962; BAS98302.1; -; Genomic_DNA.
DR   RefSeq; XP_015641629.1; XM_015786143.1.
DR   AlphaFoldDB; Q5Z5S6; -.
DR   SMR; Q5Z5S6; -.
DR   STRING; 4530.OS06T0568600-01; -.
DR   PaxDb; Q5Z5S6; -.
DR   PRIDE; Q5Z5S6; -.
DR   EnsemblPlants; Os06t0568600-01; Os06t0568600-01; Os06g0568600.
DR   GeneID; 4341340; -.
DR   Gramene; Os06t0568600-01; Os06t0568600-01; Os06g0568600.
DR   KEGG; osa:4341340; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_4_0_1; -.
DR   InParanoid; Q5Z5S6; -.
DR   OMA; HTFTKWS; -.
DR   OrthoDB; 702827at2759; -.
DR   BRENDA; 1.14.14.86; 8948.
DR   Proteomes; UP000000763; Chromosome 6.
DR   Proteomes; UP000059680; Chromosome 6.
DR   Genevisible; Q5Z5S6; OS.
DR   GO; GO:0009707; C:chloroplast outer membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0052615; F:ent-kaurene oxidase activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR   GO; GO:0010241; P:ent-kaurene oxidation to kaurenoic acid; IBA:GO_Central.
DR   GO; GO:0009686; P:gibberellin biosynthetic process; IBA:GO_Central.
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   InterPro; IPR044225; KO_chloroplastic.
DR   PANTHER; PTHR47283; PTHR47283; 1.
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   2: Evidence at transcript level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..503
FT                   /note="Ent-kaurene oxidase-like 5"
FT                   /id="PRO_0000430732"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         448
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:P04798"
FT   CONFLICT        41
FT                   /note="V -> D (in Ref. 1; AAT81229)"
FT   CONFLICT        148
FT                   /note="H -> R (in Ref. 1; AAT81229)"
FT   CONFLICT        484
FT                   /note="M -> T (in Ref. 1; AAT81229)"
SQ   SEQUENCE   503 AA;  56160 MW;  FCA4325919467D45 CRC64;
     MESLLAAGAG GIGVAAAAAV VAATLAVVPP KDRGNNPPPA VPGLPVIGNM HQLKEKKPHH
     TFTKWSKTYG PIYTIKTGAS SVVVLNSTEV AKEAMIEKFS SISTKKLPKA LSVISRKNMV
     SISDYGDFYK MAKRNIMLAI LGFNAQKHFC DTRERMVSNV LSSLHKLVAV DPHSPLNFRE
     VYTTELFGLS LIQNLGEDVC SVYVEEFGRE ISKEEIFHVL VHEILSCVVE PDWRDYFPYL
     SWLPNKSFET IVSSTEFRRD AVMNALIKRQ KERIARGEAR ISYIDFLLEA KNSTQLTDHQ
     LMLLLAESIA AAVDTVLVTT EWAMYELAKN PDKQEWLYRE IREVCGGKAV TEEDLPRLPY
     LDAVLHETLR LHSPVPVLPT RFVHDDTTLA GYDVPAGTQV MINVFGCHMD EEAWESPGEW
     SPERFLGEGF KLADRYKTLA FGAGRRTCAG SQQAVSIACV AIARFVQELQ WTLREGDGDK
     EDTMQYTALK LHPLHVHLKP RGS