ABAH2_ARATH
ID ABAH2_ARATH Reviewed; 482 AA.
AC O81077;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 149.
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 707A2;
GN Name=CYP707A2; OrderedLocusNames=At2g29090; ORFNames=T9I4.17;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION, FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP 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 [5]
RP FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16543410; DOI=10.1104/pp.106.079475;
RA Okamoto M., Kuwahara A., Seo M., Kushiro T., Asami T., Hirai N., Kamiya Y.,
RA Koshiba T., Nambara E.;
RT "CYP707A1 and CYP707A2, which encode abscisic acid 8'-hydroxylases, are
RT indispensable for proper control of seed dormancy and germination in
RT Arabidopsis.";
RL Plant Physiol. 141:97-107(2006).
RN [6]
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 seed
CC dormancy and germination. {ECO:0000269|PubMed:15044947,
CC ECO:0000269|PubMed:16543410}.
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: Mainly expressed in dry seeds. Lower expression in
CC rosette leaves, flowers, siliques and stems. Not expressed in roots.
CC Expressed in both endosperm and vascular tissues of embryo during the
CC seed development and in cortex and endodermis in germinating embryo.
CC {ECO:0000269|PubMed:15044947, ECO:0000269|PubMed:16543410}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated from late-maturation to mature dry
CC seed. Up-regulated immediately after seed imbibition, reaching a
CC maximum at 6 hours and decreasing therafter.
CC {ECO:0000269|PubMed:15044947, ECO:0000269|PubMed:16543410}.
CC -!- INDUCTION: By abscisic acid, dehydration and rehydration. Expression
CC regulated by phytochrome B. {ECO:0000269|PubMed:15044947,
CC ECO:0000269|PubMed:17010113}.
CC -!- DISRUPTION PHENOTYPE: Plants show a hyperdormancy phenotype.
CC {ECO:0000269|PubMed:16543410}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AC005315; AAC33235.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08209.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08210.1; -; Genomic_DNA.
DR EMBL; AK230466; BAF02260.1; -; mRNA.
DR PIR; T02739; T02739.
DR RefSeq; NP_001189629.1; NM_001202700.1.
DR RefSeq; NP_180473.1; NM_128466.4.
DR AlphaFoldDB; O81077; -.
DR SMR; O81077; -.
DR BioGRID; 2807; 13.
DR IntAct; O81077; 13.
DR STRING; 3702.AT2G29090.1; -.
DR PaxDb; O81077; -.
DR PRIDE; O81077; -.
DR EnsemblPlants; AT2G29090.1; AT2G29090.1; AT2G29090.
DR EnsemblPlants; AT2G29090.2; AT2G29090.2; AT2G29090.
DR GeneID; 817457; -.
DR Gramene; AT2G29090.1; AT2G29090.1; AT2G29090.
DR Gramene; AT2G29090.2; AT2G29090.2; AT2G29090.
DR KEGG; ath:AT2G29090; -.
DR Araport; AT2G29090; -.
DR TAIR; locus:2066138; AT2G29090.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_15_5_1; -.
DR OMA; DDTRQMP; -.
DR OrthoDB; 871849at2759; -.
DR PhylomeDB; O81077; -.
DR BioCyc; ARA:AT2G29090-MON; -.
DR BioCyc; MetaCyc:AT2G29090-MON; -.
DR BRENDA; 1.14.14.137; 399.
DR UniPathway; UPA00093; -.
DR PRO; PR:O81077; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O81077; baseline and differential.
DR Genevisible; O81077; 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:0046345; P:abscisic acid catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009687; P:abscisic acid metabolic process; IMP:TAIR.
DR GO; GO:0048838; P:release of seed from dormancy; IMP:TAIR.
DR GO; GO:0010114; P:response to red light; IEP:TAIR.
DR GO; GO:0009639; P:response to red or far red light; IEP: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 2: Evidence at transcript level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Stress response; Transmembrane; Transmembrane helix.
FT CHAIN 1..482
FT /note="Abscisic acid 8'-hydroxylase 2"
FT /id="PRO_0000288640"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 431
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 482 AA; 55176 MW; AB6A07AB2778DD3B CRC64;
MQISSSSSSN FFSSLYADEP ALITLTIVVV VVVLLFKWWL HWKEQRLRLP PGSMGLPYIG
ETLRLYTENP NSFFATRQNK YGDIFKTHIL GCPCVMISSP EAARMVLVSK AHLFKPTYPP
SKERMIGPEA LFFHQGPYHS TLKRLVQSSF MPSALRPTVS HIELLVLQTL SSWTSQKSIN
TLEYMKRYAF DVAIMSAFGD KEEPTTIDVI KLLYQRLERG YNSMPLDLPG TLFHKSMKAR
IELSEELRKV IEKRRENGRE EGGLLGVLLG AKDQKRNGLS DSQIADNIIG VIFAATDTTA
SVLTWLLKYL HDHPNLLQEV SREQFSIRQK IKKENRRISW EDTRKMPLTT RVIQETLRAA
SVLSFTFREA VQDVEYDGYL IPKGWKVLPL FRRIHHSSEF FPDPEKFDPS RFEVAPKPYT
YMPFGNGVHS CPGSELAKLE MLILLHHLTT SFRWEVIGDE EGIQYGPFPV PKKGLPIRVT
PI
