ABAH1_ORYSI
ID ABAH1_ORYSI Reviewed; 471 AA.
AC Q09J79;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Abscisic acid 8'-hydroxylase 1;
DE Short=ABA 8'-hydroxylase 1;
DE EC=1.14.14.137 {ECO:0000250|UniProtKB:Q949P1};
DE AltName: Full=Cytochrome P450 707A5;
DE AltName: Full=OsABA8ox1;
GN Name=CYP707A5; Synonyms=ABA8OX1; ORFNames=OsI_008437;
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 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 seedlings and expanding leaves.
CC {ECO:0000269|PubMed:17022939}.
CC -!- INDUCTION: By ethylene or abscisic acid treatments, and salt or osmotic
CC stresses. {ECO:0000269|PubMed:17022939}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; DQ887714; ABI64254.1; -; mRNA.
DR EMBL; CM000127; EAY87204.1; -; Genomic_DNA.
DR AlphaFoldDB; Q09J79; -.
DR SMR; Q09J79; -.
DR STRING; 39946.Q09J79; -.
DR EnsemblPlants; BGIOSGA008883-TA; BGIOSGA008883-PA; BGIOSGA008883.
DR Gramene; BGIOSGA008883-TA; BGIOSGA008883-PA; BGIOSGA008883.
DR HOGENOM; CLU_001570_15_5_1; -.
DR OMA; AHMCLGL; -.
DR UniPathway; UPA00093; -.
DR Proteomes; UP000007015; Chromosome 2.
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; Stress response; Transmembrane; Transmembrane helix.
FT CHAIN 1..471
FT /note="Abscisic acid 8'-hydroxylase 1"
FT /id="PRO_0000288643"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 415
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 471 AA; 52920 MW; 24D4FB1BC5A62BE9 CRC64;
MGAFLLFVCV LAPFLLVCAV RGRRRQAGSS EAAACGLPLP PGSMGWPYVG ETFQLYSSKN
PNVFFNKKRN KYGPIFKTHI LGCPCVMVSS PEAARFVLVT QAHLFKPTFP ASKERMLGPQ
AIFFQQGDYH AHLRRIVSRA FSPESIRASV PAIEAIALRS LHSWDGQFVN TFQEMKTYAL
NVALLSIFGE EEMRYIEELK QCYLTLEKGY NSMPVNLPGT LFHKAMKARK RLGAIVAHII
SARRERQRGN DLLGSFVDGR EALTDAQIAD NVIGVIFAAR DTTASVLTWM VKFLGDHPAV
LKAVTEEQLQ IAKEKEASGE PLSWADTRRM KMTSRVIQET MRVASILSFT FREAVEDVEY
QGYLIPKGWK VLPLFRNIHH NPDHFPCPEK FDPSRFEVAP KPNTFMPFGN GTHSCPGNEL
AKLEMLVLFH HLATKYRWST SKSESGVQFG PFALPLNGLP MSFTRKNTEQ E
