ABAH2_ORYSI
ID ABAH2_ORYSI Reviewed; 506 AA.
AC Q09J78; A2YW59;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
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; ORFNames=OsI_028552;
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND LACK OF
RP INDUCTION.
RC STRAIN=cv. Pin Gaew 56;
RX PubMed=17022939; DOI=10.1016/j.bbrc.2006.09.098;
RA Yang S.-H., Choi D.;
RT "Characterization of genes encoding ABA 8'-hydroxylase in ethylene-induced
RT stem growth of deepwater rice (Oryza sativa L.).";
RL Biochem. Biophys. Res. Commun. 350:685-690(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
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).
CC -!- FUNCTION: Involved in the oxidative degradation of abscisic acid.
CC {ECO:0000269|PubMed:17022939}.
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 -!- TISSUE SPECIFICITY: In internodes and expanding leaves. Weak expression
CC in seedlings. {ECO:0000269|PubMed:17022939}.
CC -!- INDUCTION: Not induced by ethylene or abscisic acid treatments, and
CC salt or osmotic stresses.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; DQ887715; ABI64255.1; -; mRNA.
DR EMBL; CM000133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q09J78; -.
DR SMR; Q09J78; -.
DR STRING; 39946.Q09J78; -.
DR EnsemblPlants; BGIOSGA026823-TA; BGIOSGA026823-PA; BGIOSGA026823.
DR Gramene; BGIOSGA026823-TA; BGIOSGA026823-PA; BGIOSGA026823.
DR HOGENOM; CLU_001570_15_5_1; -.
DR OMA; KFVFANA; -.
DR UniPathway; UPA00093; -.
DR Proteomes; UP000007015; Chromosome 8.
DR ExpressionAtlas; Q09J78; differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0010295; F:(+)-abscisic acid 8'-hydroxylase activity; IEA:UniProtKB-EC.
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 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..506
FT /note="Abscisic acid 8'-hydroxylase 2"
FT /id="PRO_0000288645"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 437
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 506 AA; 56327 MW; F29DB8BD2C3D327F 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 GGGDDLLGGL MRSRDDGTAG AVALLTDDQI ADNVVGVLFA
AQDTTASVLT WILKYLHDSP KLLEAVKAEQ MAIYVANEGG KRPLTWTQTR SMTLTHQVIL
ESLRMASIIS FTFREAVADV EYKGFLIPKG WKVMPLFRNI HHNPDYFQDP QKFDPSRFKV
APRPSTFLPF GSGVHACPGN ELAKLEMLVL VHRLVTAYRW EIVGASDEVE YSPFPVPRGG
LNAKLWKQEA EEDMYMAMGT ITAAGA
