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 24-JAN-2024, entry version 128. 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 CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:12897, Rhea:RHEA- CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:37569, CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58490; CC EC=1.14.14.137; 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}; 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; 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; 39947.Q6ZDE3; -. DR PaxDb; 39947-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; WKETRSQ; -. DR OrthoDB; 758626at2759; -. 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 GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. 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:0046345; P:abscisic acid catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central. DR CDD; cd11043; CYP90-like; 1. DR Gene3D; 1.10.630.10; Cytochrome P450; 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 PANTHER; PTHR24286:SF354; ABSCISIC ACID 8'-HYDROXYLASE 2; 1. DR PANTHER; PTHR24286; CYTOCHROME P450 26; 1. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; Cytochrome P450; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. DR Genevisible; Q6ZDE3; OS. 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 //