ABAH2_ORYSJ
ID ABAH2_ORYSJ Reviewed; 510 AA.
AC Q6ZDE3; A0A0P0XGQ2; A3BU19;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Abscisic acid 8'-hydroxylase 2;
DE Short=ABA 8'-hydroxylase 2;
DE EC=1.14.14.137 {ECO:0000250|UniProtKB:Q949P1};
DE AltName: Full=Cytochrome P450 707A6;
DE AltName: Full=OsABA8ox2;
GN Name=CYP707A6; Synonyms=ABA8OX2;
GN OrderedLocusNames=Os08g0472800, LOC_Os08g36860;
GN ORFNames=OsJ_026541, P0013B04.19;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP IDENTIFICATION, AND LACK OF INDUCTION.
RC STRAIN=cv. Nipponbare;
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 -!- 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=EAZ43058.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP004457; BAD09367.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF23935.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT05855.1; -; Genomic_DNA.
DR EMBL; CM000145; EAZ43058.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK120757; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015648451.1; XM_015792965.1.
DR AlphaFoldDB; Q6ZDE3; -.
DR SMR; Q6ZDE3; -.
DR STRING; 4530.OS08T0472800-01; -.
DR PaxDb; Q6ZDE3; -.
DR PRIDE; Q6ZDE3; -.
DR EnsemblPlants; Os08t0472800-01; Os08t0472800-01; Os08g0472800.
DR GeneID; 4345810; -.
DR Gramene; Os08t0472800-01; Os08t0472800-01; Os08g0472800.
DR KEGG; osa:4345810; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_15_5_1; -.
DR InParanoid; Q6ZDE3; -.
DR OMA; KFVFANA; -.
DR OrthoDB; 864748at2759; -.
DR BRENDA; 1.14.14.137; 4460.
DR UniPathway; UPA00093; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000007752; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR Genevisible; Q6ZDE3; OS.
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..510
FT /note="Abscisic acid 8'-hydroxylase 2"
FT /id="PRO_0000288646"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 441
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 CONFLICT 430
FT /note="T -> S (in Ref. 5; AK120757)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 510 AA; 56556 MW; C1F583725741091E CRC64;
MAFLLFFVFV TAAVLCFVVP AFLLLCTSVQ RRRDVGQGGG RDWQKKKKLR LPPGSMGWPY
VGETLQLYSQ DPNVFFASKQ KRYGEIFKTN LLGCPCVMLA SPEAARFVLV SQARLFKPTY
PPSKERMIGP SALFFHQGEY HLRLRRLVQA ALAPDSLRAL VPDVDAAVAA TLAAWSGGHV
ASTFHAMKKL SFDVGVVTIF GGRLGRRHRE ELRTNYSVVE RGYNCFPNRF PGTLYHKAIQ
ARKRLRAILS EIVAERRARG GGGGGGGDDL LGGLMRSRDD GTAGAVALLT DDQIADNVVG
VLFAAQDTTA SVLTWILKYL HDSPKLLEAV KAEQMAIYVA NEGGKRPLTW TQTRSMTLTH
QVILESLRMA SIISFTFREA VADVEYKGFL IPKGWKVMPL FRNIHHNPDY FQDPQKFDPS
RFKVAPRPST FLPFGSGVHA CPGNELAKLE MLVLVHRLVT AYRWEIVGAS DEVEYSPFPV
PRGGLNAKLW KQEAEEDMYM AMGTITAAGA
