ABAH1_ARATH
ID ABAH1_ARATH Reviewed; 467 AA.
AC Q949P1; O65624;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Abscisic acid 8'-hydroxylase 1;
DE Short=ABA 8'-hydroxylase 1;
DE EC=1.14.14.137 {ECO:0000269|PubMed:15064374};
DE AltName: Full=Cytochrome P450 707A1;
GN Name=CYP707A1; OrderedLocusNames=At4g19230; ORFNames=T18B16.200;
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], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP 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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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].
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, 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 [6]
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 [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. Plays
CC an important role in determining abscisic acid levels in dry seeds and
CC in the control of postgermination growth. {ECO:0000269|PubMed:15044947,
CC ECO:0000269|PubMed:15064374, 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:0000269|PubMed:15064374};
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q949P1-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Mainly expressed in flowers, siliques, roots and
CC stems. Lower expression in rosette leaves and dry seeds. Expressed in
CC vascular tissues of embryo during the seed development.
CC {ECO:0000269|PubMed:15044947, ECO:0000269|PubMed:15064374,
CC ECO:0000269|PubMed:16543410}.
CC -!- DEVELOPMENTAL STAGE: Expressed predominantly during mid-maturation of
CC seed and down-regulated during late maturation. Up-regulated 12 hours
CC after seed imbibition. {ECO:0000269|PubMed:15044947,
CC ECO:0000269|PubMed:16543410}.
CC -!- INDUCTION: By abscisic acid treatment, salt or osmotic stresses, and by
CC dehydration and rehydration. Expression regulated by phytochrome B.
CC {ECO:0000269|PubMed:15044947, ECO:0000269|PubMed:15064374,
CC ECO:0000269|PubMed:17010113}.
CC -!- DISRUPTION PHENOTYPE: Plants show a reduced germination.
CC {ECO:0000269|PubMed:16543410}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16713.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78925.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB122149; BAD16629.1; -; mRNA.
DR EMBL; AL021687; CAA16713.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161550; CAB78925.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84162.1; -; Genomic_DNA.
DR EMBL; AY050980; AAK93657.1; -; mRNA.
DR EMBL; AY091446; AAM14385.1; -; mRNA.
DR PIR; T04444; T04444.
DR RefSeq; NP_567581.1; NM_118043.2. [Q949P1-1]
DR AlphaFoldDB; Q949P1; -.
DR SMR; Q949P1; -.
DR BioGRID; 12956; 1.
DR STRING; 3702.AT4G19230.2; -.
DR PRIDE; Q949P1; -.
DR EnsemblPlants; AT4G19230.1; AT4G19230.1; AT4G19230. [Q949P1-1]
DR GeneID; 827663; -.
DR Gramene; AT4G19230.1; AT4G19230.1; AT4G19230. [Q949P1-1]
DR KEGG; ath:AT4G19230; -.
DR Araport; AT4G19230; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_15_5_1; -.
DR OMA; AHMCLGL; -.
DR PhylomeDB; Q949P1; -.
DR BioCyc; ARA:AT4G19230-MON; -.
DR BioCyc; MetaCyc:AT4G19230-MON; -.
DR BRENDA; 1.14.14.137; 399.
DR UniPathway; UPA00093; -.
DR PRO; PR:Q949P1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q949P1; baseline and differential.
DR Genevisible; Q949P1; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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; IEA:UniProtKB-UniPathway.
DR GO; GO:0009687; P:abscisic acid metabolic process; IBA:GO_Central.
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 NADP; Oxidoreductase; Reference proteome; Stress response; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..467
FT /note="Abscisic acid 8'-hydroxylase 1"
FT /id="PRO_0000288639"
FT TRANSMEM 5..24
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"
SQ SEQUENCE 467 AA; 53037 MW; 2F4230446536D955 CRC64;
MDISALFLTL FAGSLFLYFL RCLISQRRFG SSKLPLPPGT MGWPYVGETF QLYSQDPNVF
FQSKQKRYGS VFKTHVLGCP CVMISSPEAA KFVLVTKSHL FKPTFPASKE RMLGKQAIFF
HQGDYHAKLR KLVLRAFMPE SIRNMVPDIE SIAQDSLRSW EGTMINTYQE MKTYTFNVAL
LSIFGKDEVL YREDLKRCYY ILEKGYNSMP VNLPGTLFHK SMKARKELSQ ILARILSERR
QNGSSHNDLL GSFMGDKEEL TDEQIADNII GVIFAARDTT ASVMSWILKY LAENPNVLEA
VTEEQMAIRK DKEEGESLTW GDTKKMPLTS RVIQETLRVA SILSFTFREA VEDVEYEGYL
IPKGWKVLPL FRNIHHSADI FSNPGKFDPS RFEVAPKPNT FMPFGNGTHS CPGNELAKLE
MSIMIHHLTT KYSWSIVGAS DGIQYGPFAL PQNGLPIVLA RKPEIEV
