ABAH3_ORYSJ
ID ABAH3_ORYSJ Reviewed; 500 AA.
AC Q0J185; A0A0P0XNJ5; Q67TP6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Abscisic acid 8'-hydroxylase 3;
DE Short=ABA 8'-hydroxylase 3;
DE EC=1.14.14.137 {ECO:0000250|UniProtKB:Q949P1};
DE AltName: Full=Cytochrome P450 707A7;
DE AltName: Full=OsABA8ox3;
GN Name=CYP707A7; Synonyms=ABA8OX3;
GN OrderedLocusNames=Os09g0457100, LOC_Os09g28390;
GN ORFNames=B1342C04.43, OsJ_028469;
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 [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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP IDENTIFICATION, AND LACK OF INDUCTION.
RX PubMed=17205969; DOI=10.1093/pcp/pcm003;
RA Saika H., Okamoto M., Miyoshi K., Kushiro T., Shinoda S., Jikumaru Y.,
RA Fujimoto M., Arikawa T., Takahashi H., Ando M., Arimura S., Miyao A.,
RA Hirochika H., Kamiya Y., Tsutsumi N., Nambara E., Nakazono M.;
RT "Ethylene promotes submergence-induced expression of OsABA8ox1, a gene that
RT encodes ABA 8'-hydroxylase in rice.";
RL Plant Cell Physiol. 48:287-298(2007).
CC -!- FUNCTION: Involved in the oxidative degradation of abscisic acid.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-cis-(+)-abscisate + O2 + reduced [NADPH--hemoprotein
CC reductase] = (+)-8'-hydroxyabscisate + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:12897, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:37569, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:58490; EC=1.14.14.137;
CC Evidence={ECO:0000250|UniProtKB:Q949P1};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- PATHWAY: Plant hormone degradation; abscisic acid degradation.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Not induced by ethylene treatment or flooding.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD38475.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP006057; BAD38475.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008215; BAF25280.1; -; Genomic_DNA.
DR EMBL; AP014965; BAT08439.1; -; Genomic_DNA.
DR EMBL; CM000146; EAZ44986.1; -; Genomic_DNA.
DR RefSeq; XP_015610835.1; XM_015755349.1.
DR AlphaFoldDB; Q0J185; -.
DR SMR; Q0J185; -.
DR STRING; 4530.OS09T0457100-01; -.
DR PaxDb; Q0J185; -.
DR PRIDE; Q0J185; -.
DR EnsemblPlants; Os09t0457100-01; Os09t0457100-01; Os09g0457100.
DR GeneID; 4347261; -.
DR Gramene; Os09t0457100-01; Os09t0457100-01; Os09g0457100.
DR KEGG; osa:4347261; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_15_5_1; -.
DR InParanoid; Q0J185; -.
DR OMA; HLECSYR; -.
DR OrthoDB; 871849at2759; -.
DR BRENDA; 1.14.14.137; 4460.
DR PlantReactome; R-OSA-1119609; Phaseic acid biosynthesis.
DR UniPathway; UPA00093; -.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000007752; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0010295; F:(+)-abscisic acid 8'-hydroxylase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0046345; P:abscisic acid catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016125; P:sterol metabolic 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 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..500
FT /note="Abscisic acid 8'-hydroxylase 3"
FT /id="PRO_0000288648"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 426
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"
SQ SEQUENCE 500 AA; 56167 MW; 8F4D0470C0644203 CRC64;
MAASFVIVIV ISFFISLAFM CYVHYTSRQR RKLHGYGHEK AVRLPPGSMG WPYIGETLQL
YSQDPNVFFA SKQKRYGEIF KTHILGCPCV MLASPEAARF VLVTQAHLFK PTYPRSKERM
IGPSALFFHQ GDYHLRLRKL VQGPLGPDAL RALVPDVEAA VRSTLASWDG NVSSTFHAMK
RLSFDVGIVT IFGGRLDERR KAELRQNYAI VEKGYNSFPN SFPGTLYYKA IQARRRLHGV
LSDIMRERRA RGEPGSDLLG CLMQSRAGDD GALLTDEQVA DNIIGVLFAA QDTTASVLTW
IVKYLHDHPK LLEAVRAEQA AIRAANDGGR LPLTWAQTRS MALTHKVILE SLRMASIISF
TFREAVADVE YKGFLIPKGW KVMPLFRNIH HNPDYFQDPQ KFDPSRFKVS PRPNTFMPFG
NGVHACPGNE LAKLEMLVLI HHLVTGYRWE IVGSSDEVEY SPFPVPKHGL LAKLWRDDSV
SVETDGCQNG DNDDNGVAMV
