ABAH4_ARATH
ID ABAH4_ARATH Reviewed; 468 AA.
AC Q9LJK2; Q8LF37;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Abscisic acid 8'-hydroxylase 4;
DE Short=ABA 8'-hydroxylase 4;
DE EC=1.14.14.137 {ECO:0000250|UniProtKB:Q949P1};
DE AltName: Full=Cytochrome P450 707A4;
GN Name=CYP707A4; OrderedLocusNames=At3g19270; ORFNames=MVI11.19;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) 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, AND TISSUE SPECIFICITY.
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).
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). {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 flowers. Lower expression in
CC siliques, rosette leaves, roots and stems. Not expressed in dry seeds.
CC Expressed in silique envelopes, but not in embryo or endosperm during
CC the seed development. {ECO:0000269|PubMed:15044947,
CC ECO:0000269|PubMed:16543410}.
CC -!- DEVELOPMENTAL STAGE: Not induced after imbibition.
CC {ECO:0000269|PubMed:15044947, ECO:0000269|PubMed:16543410}.
CC -!- INDUCTION: By abscisic acid, dehydration and rehydration.
CC {ECO:0000269|PubMed:15044947}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02968.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP000419; BAB02968.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; ANM64023.1; -; Genomic_DNA.
DR EMBL; AY085068; AAM61624.1; -; mRNA.
DR RefSeq; NP_001319589.1; NM_001338388.1.
DR RefSeq; NP_566628.1; NM_112814.2.
DR AlphaFoldDB; Q9LJK2; -.
DR SMR; Q9LJK2; -.
DR STRING; 3702.AT3G19270.1; -.
DR PaxDb; Q9LJK2; -.
DR PRIDE; Q9LJK2; -.
DR EnsemblPlants; AT3G19270.2; AT3G19270.2; AT3G19270.
DR GeneID; 821461; -.
DR Gramene; AT3G19270.2; AT3G19270.2; AT3G19270.
DR KEGG; ath:AT3G19270; -.
DR Araport; AT3G19270; -.
DR TAIR; locus:2094058; AT3G19270.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_15_5_1; -.
DR OMA; KFVFANA; -.
DR OrthoDB; 871849at2759; -.
DR PhylomeDB; Q9LJK2; -.
DR BioCyc; ARA:AT3G19270-MON; -.
DR BioCyc; MetaCyc:AT3G19270-MON; -.
DR BRENDA; 1.14.14.137; 399.
DR UniPathway; UPA00093; -.
DR PRO; PR:Q9LJK2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJK2; baseline and differential.
DR Genevisible; Q9LJK2; 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: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..468
FT /note="Abscisic acid 8'-hydroxylase 4"
FT /id="PRO_0000288642"
FT TRANSMEM 4..24
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 468 AA; 53922 MW; 0D9FA04292C062C7 CRC64;
MAEIWFLVVP ILILCLLLVR VIVSKKKKNS RGKLPPGSMG WPYLGETLQL YSQNPNVFFT
SKQKRYGEIF KTRILGYPCV MLASPEAARF VLVTHAHMFK PTYPRSKEKL IGPSALFFHQ
GDYHSHIRKL VQSSFYPETI RKLIPDIEHI ALSSLQSWAN MPIVSTYQEM KKFAFDVGIL
AIFGHLESSY KEILKHNYNI VDKGYNSFPM SLPGTSYHKA LMARKQLKTI VSEIICERRE
KRALQTDFLG HLLNFKNEKG RVLTQEQIAD NIIGVLFAAQ DTTASCLTWI LKYLHDDQKL
LEAVKAEQKA IYEENSREKK PLTWRQTRNM PLTHKVIVES LRMASIISFT FREAVVDVEY
KGYLIPKGWK VMPLFRNIHH NPKYFSNPEV FDPSRFEVNP KPNTFMPFGS GVHACPGNEL
AKLQILIFLH HLVSNFRWEV KGGEKGIQYS PFPIPQNGLP ATFRRHSL
