ABAH2_SOLLC
ID ABAH2_SOLLC Reviewed; 469 AA.
AC K4CI52; G3CKB8;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Abscisic acid 8'-hydroxylase CYP707A2 {ECO:0000305};
DE Short=ABA 8'-hydroxylase CYP707A2 {ECO:0000305};
DE Short=SlCYP707A2 {ECO:0000303|PubMed:25039074};
DE EC=1.14.14.137 {ECO:0000250|UniProtKB:Q949P1};
DE AltName: Full=Cytochrome P450 707A2 {ECO:0000303|PubMed:25039074};
GN Name=CYP707A2 {ECO:0000303|PubMed:25039074};
GN OrderedLocusNames=Solyc08g005610.2.1 {ECO:0000305};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 78-382.
RA Leng P., Sun L.;
RT "Cloning and expression analysis of Solanum lycopersicum ABA 8'-hydroxylase
RT CYP707A2 gene.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP INDUCTION BY ABSCISIC ACID AND DEHYDRATION, AND PATHWAY.
RC STRAIN=cv. Jia Bao;
RX PubMed=25039074; DOI=10.1093/jxb/eru288;
RA Ji K., Kai W., Zhao B., Sun Y., Yuan B., Dai S., Li Q., Chen P., Wang Y.,
RA Pei Y., Wang H., Guo Y., Leng P.;
RT "SlNCED1 and SlCYP707A2: key genes involved in ABA metabolism during tomato
RT fruit ripening.";
RL J. Exp. Bot. 65:5243-5255(2014).
CC -!- FUNCTION: Negative regulator of fruit ripening involved in the
CC oxidative degradation of abscisic acid (ABA).
CC {ECO:0000269|PubMed:25039074}.
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;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- PATHWAY: Plant hormone degradation; abscisic acid degradation.
CC {ECO:0000269|PubMed:25039074}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in fruit.
CC {ECO:0000269|PubMed:25039074}.
CC -!- DEVELOPMENTAL STAGE: Fluctuant expression pattern with four peaks
CC during development, and then it increased rapidly during ripening.
CC {ECO:0000269|PubMed:25039074}.
CC -!- INDUCTION: First transiently repressed (1 day after treatment) and
CC later induced (2 days after treatment) by abscisic acid (ABA) and
CC dehydration. {ECO:0000269|PubMed:25039074}.
CC -!- DISRUPTION PHENOTYPE: Silenced plants fruits have a rapid ripening with
CC a quick colouring and associated with higher abscisic acid (ABA)
CC levels. When disrupted in fruits, altered expression of ABA-responsive
CC and ripening-related genes. {ECO:0000269|PubMed:25039074}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; CM001071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; HQ008774; AEK99073.1; -; mRNA.
DR RefSeq; XP_004244436.1; XM_004244388.3.
DR AlphaFoldDB; K4CI52; -.
DR SMR; K4CI52; -.
DR STRING; 4081.Solyc08g005610.2.1; -.
DR PaxDb; K4CI52; -.
DR PRIDE; K4CI52; -.
DR EnsemblPlants; Solyc08g005610.3.1; Solyc08g005610.3.1; Solyc08g005610.3.
DR GeneID; 101249565; -.
DR Gramene; Solyc08g005610.3.1; Solyc08g005610.3.1; Solyc08g005610.3.
DR KEGG; sly:101249565; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_15_5_1; -.
DR InParanoid; K4CI52; -.
DR OMA; WPLRTFA; -.
DR OrthoDB; 574756at2759; -.
DR PhylomeDB; K4CI52; -.
DR UniPathway; UPA00093; -.
DR Proteomes; UP000004994; Chromosome 8.
DR ExpressionAtlas; K4CI52; baseline and differential.
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: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; IMP:UniProtKB.
DR GO; GO:0009687; P:abscisic acid metabolic process; IBA:GO_Central.
DR GO; GO:0009835; P:fruit ripening; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
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; Transmembrane; Transmembrane helix.
FT CHAIN 1..469
FT /note="Abscisic acid 8'-hydroxylase CYP707A2"
FT /id="PRO_0000445690"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 414
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|UniProtKB:Q96242"
SQ SEQUENCE 469 AA; 53251 MW; 2589D35974346A2C CRC64;
MEFVSMLCLF TFISLTLLLI HSIFKFLAFA SKKLPLPPGT LGLPYIGETF QLYSQNPNVF
FASKVKKYGS IFKTYILGCP CVMISSPEAA KQVLVTKANL FKPTFPASKE RMLGKQAIFF
HQGDYHAKLR KLVLQAFKPD SIRNIIPDIE SIAITSLESF QGRLINTYQE MKTYTFNVAL
ISIFGKDEFL YREELKKCYY ILEKGYNSMP INLPGTLFNK AMKARKELAK IVAKIISTRR
EMKIDHGDLL GSFMGDKEGL TDEQIADNVI GVIFAARDTT ASVLTWILKY LGENPSVLQA
VTEEQENIMR KKEVNGEEKV LNWQDTRQMP MTTRVIQETL RVASILSFTF REAVEDVEFE
GYLIPKGWKV LPLFRNIHHS PDNFPEPEKF DPSRFEVSPK PNTFMPFGNG VHSCPGNDLA
KLEILILVHH LTTKYRWSMV GPQNGIQYGP FALPQNGLPI KLSLKTSST
