ABAH3_ARATH
ID ABAH3_ARATH Reviewed; 463 AA.
AC Q9FH76; Q3E8G7;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
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 707A3;
GN Name=CYP707A3; OrderedLocusNames=At5g45340; ORFNames=K9E15.12;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15064374; DOI=10.1104/pp.103.037614;
RA Saito S., Hirai N., Matsumoto C., Ohigashi H., Ohta D., Sakata K.,
RA Mizutani M.;
RT "Arabidopsis CYP707As encode (+)-abscisic acid 8'-hydroxylase, a key enzyme
RT in the oxidative catabolism of abscisic acid.";
RL Plant Physiol. 134:1439-1449(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP IDENTIFICATION, FUNCTION, MUTAGENESIS OF CYS-411, ACTIVITY REGULATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=15044947; DOI=10.1038/sj.emboj.7600121;
RA Kushiro T., Okamoto M., Nakabayashi K., Yamagishi K., Kitamura S.,
RA Asami T., Hirai N., Koshiba T., Kamiya Y., Nambara E.;
RT "The Arabidopsis cytochrome P450 CYP707A encodes ABA 8'-hydroxylases: key
RT enzymes in ABA catabolism.";
RL EMBO J. 23:1647-1656(2004).
RN [6]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16623881; DOI=10.1111/j.1365-313x.2006.02683.x;
RA Umezawa T., Okamoto M., Kushiro T., Nambara E., Oono Y., Seki M.,
RA Kobayashi M., Koshiba T., Kamiya Y., Shinozaki K.;
RT "CYP707A3, a major ABA 8'-hydroxylase involved in dehydration and
RT rehydration response in Arabidopsis thaliana.";
RL Plant J. 46:171-182(2006).
RN [7]
RP INDUCTION BY PHYTOCHROME B.
RX PubMed=17010113; DOI=10.1111/j.1365-313x.2006.02881.x;
RA Seo M., Hanada A., Kuwahara A., Endo A., Okamoto M., Yamauchi Y., North H.,
RA Marion-Poll A., Sun T.P., Koshiba T., Kamiya Y., Yamaguchi S., Nambara E.;
RT "Regulation of hormone metabolism in Arabidopsis seeds: phytochrome
RT regulation of abscisic acid metabolism and abscisic acid regulation of
RT gibberellin metabolism.";
RL Plant J. 48:354-366(2006).
CC -!- FUNCTION: Involved in the oxidative degradation of abscisic acid, but
CC not in the isomerization of the produced 8'-hydroxyabscisic acid (8'-
CC OH-ABA) to (-)-phaseic acid (PA). Involved in the control of
CC postgermination growth. {ECO:0000269|PubMed:15044947,
CC ECO:0000269|PubMed:15064374, ECO:0000269|PubMed:16623881}.
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 -!- ACTIVITY REGULATION: Inhibited by tetcyclcis, but not by metyrapone.
CC {ECO:0000269|PubMed:15044947}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.3 uM for (+)-ABA {ECO:0000269|PubMed:15064374};
CC -!- PATHWAY: Plant hormone degradation; abscisic acid degradation.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FH76-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FH76-2; Sequence=VSP_025739, VSP_025740;
CC -!- TISSUE SPECIFICITY: Mainly expressed in flower buds, flowers, rosette
CC leaves and roots. Lower expression in mature siliques and inflorescence
CC stems. Not expressed in dry seeds. {ECO:0000269|PubMed:15044947,
CC ECO:0000269|PubMed:15064374}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated 12 hours after imbibition.
CC {ECO:0000269|PubMed:15044947}.
CC -!- INDUCTION: By abscisic acid, brassinosteroid or gibberellin treatments,
CC by salt or osmotic stresses, and by dehydration and rehydration.
CC Expression regulated by phytochrome B. {ECO:0000269|PubMed:15044947,
CC ECO:0000269|PubMed:15064374, ECO:0000269|PubMed:16623881,
CC ECO:0000269|PubMed:17010113}.
CC -!- DISRUPTION PHENOTYPE: Plants are not affected in seed germination, but
CC show a restricted greening rate after germination and increase the
CC drought resistance. {ECO:0000269|PubMed:16623881}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AB122150; BAD16630.1; -; mRNA.
DR EMBL; AB020744; BAB10255.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95234.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95235.1; -; Genomic_DNA.
DR EMBL; AY065065; AAL57698.1; -; mRNA.
DR EMBL; AY102136; AAM26703.1; -; mRNA.
DR RefSeq; NP_199347.2; NM_123902.3. [Q9FH76-2]
DR RefSeq; NP_851136.1; NM_180805.4. [Q9FH76-1]
DR AlphaFoldDB; Q9FH76; -.
DR SMR; Q9FH76; -.
DR STRING; 3702.AT5G45340.1; -.
DR BindingDB; Q9FH76; -.
DR ChEMBL; CHEMBL4538; -.
DR iPTMnet; Q9FH76; -.
DR PaxDb; Q9FH76; -.
DR PRIDE; Q9FH76; -.
DR ProteomicsDB; 245116; -. [Q9FH76-1]
DR EnsemblPlants; AT5G45340.1; AT5G45340.1; AT5G45340. [Q9FH76-1]
DR EnsemblPlants; AT5G45340.2; AT5G45340.2; AT5G45340. [Q9FH76-2]
DR GeneID; 834570; -.
DR Gramene; AT5G45340.1; AT5G45340.1; AT5G45340. [Q9FH76-1]
DR Gramene; AT5G45340.2; AT5G45340.2; AT5G45340. [Q9FH76-2]
DR KEGG; ath:AT5G45340; -.
DR Araport; AT5G45340; -.
DR TAIR; locus:2158480; AT5G45340.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_15_5_1; -.
DR OMA; WPLRTFA; -.
DR OrthoDB; 871849at2759; -.
DR PhylomeDB; Q9FH76; -.
DR BioCyc; ARA:AT5G45340-MON; -.
DR BioCyc; MetaCyc:AT5G45340-MON; -.
DR BRENDA; 1.14.14.137; 399.
DR SABIO-RK; Q9FH76; -.
DR UniPathway; UPA00093; -.
DR PRO; PR:Q9FH76; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FH76; baseline and differential.
DR Genevisible; Q9FH76; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0010295; F:(+)-abscisic acid 8'-hydroxylase activity; IDA:TAIR.
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:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR GO; GO:0046345; P:abscisic acid catabolic process; TAS:TAIR.
DR GO; GO:0009687; P:abscisic acid metabolic process; IBA:GO_Central.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0009639; P:response to red or far red light; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
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 1: Evidence at protein level;
KW Alternative splicing; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Stress response; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..463
FT /note="Abscisic acid 8'-hydroxylase 3"
FT /id="PRO_0000288641"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 411
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 VAR_SEQ 434..447
FT /note="WSIVGPSDGIQYGP -> LVHLQNDNSPFGN (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_025739"
FT VAR_SEQ 448..463
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_025740"
FT MUTAGEN 411
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15044947"
SQ SEQUENCE 463 AA; 52367 MW; CCD17293F553F812 CRC64;
MDFSGLFLTL SAAALFLCLL RFIAGVRRSS STKLPLPPGT MGYPYVGETF QLYSQDPNVF
FAAKQRRYGS VFKTHVLGCP CVMISSPEAA KFVLVTKSHL FKPTFPASKE RMLGKQAIFF
HQGDYHSKLR KLVLRAFMPD AIRNMVPHIE SIAQESLNSW DGTQLNTYQE MKTYTFNVAL
ISILGKDEVY YREDLKRCYY ILEKGYNSMP INLPGTLFHK AMKARKELAQ ILANILSKRR
QNPSSHTDLL GSFMEDKAGL TDEQIADNII GVIFAARDTT ASVLTWILKY LADNPTVLEA
VTEEQMAIRK DKKEGESLTW EDTKKMPLTY RVIQETLRAA TILSFTFREA VEDVEYEGYL
IPKGWKVLPL FRNIHHNADI FSDPGKFDPS RFEVAPKPNT FMPFGSGIHS CPGNELAKLE
ISVLIHHLTT KYRWSIVGPS DGIQYGPFAL PQNGLPIALE RKP
