ABAH1_SOLLC
ID ABAH1_SOLLC Reviewed; 476 AA.
AC A9QNE7;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Abscisic acid 8'-hydroxylase CYP707A1 {ECO:0000305};
DE Short=ABA 8'-hydroxylase CYP707A1 {ECO:0000305};
DE Short=SlCYP707A1 {ECO:0000303|PubMed:19322584};
DE EC=1.14.14.137 {ECO:0000250|UniProtKB:Q949P1};
DE AltName: Full=Cytochrome P450 707A1 {ECO:0000303|PubMed:19322584};
GN Name=CYP707A1 {ECO:0000303|PubMed:19322584};
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION BY
RP POLLINATION; AUXIN AND ABSCISIC ACID, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Moneymaker;
RX PubMed=19322584; DOI=10.1007/s00425-009-0913-7;
RA Nitsch L.M., Oplaat C., Feron R., Ma Q., Wolters-Arts M., Hedden P.,
RA Mariani C., Vriezen W.H.;
RT "Abscisic acid levels in tomato ovaries are regulated by LeNCED1 and
RT SlCYP707A1.";
RL Planta 229:1335-1346(2009).
RN [2]
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 [3]
RP INDUCTION BY ABIOTIC STRESS.
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: Involved in the oxidative degradation of abscisic acid,
CC especially in pollinated ovaries. {ECO:0000269|PubMed:19322584}.
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:0000250|UniProtKB:Q949P1}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in ovaries (specifically in ovules and
CC placenta), sepals, petals and pedicels. {ECO:0000269|PubMed:19322584}.
CC -!- DEVELOPMENTAL STAGE: In unpollinated ovaries, present in the placenta,
CC but not in ovules and pericarp. In pollinated ovaries, accumulates
CC mostly in the placenta and ovules and, at low levels, in the pericarp.
CC {ECO:0000269|PubMed:19322584}.
CC -!- INDUCTION: Accumulates strongly after pollination in whole ovaries.
CC Induced by auxin (4-Cl-IAA) treatment and abscisic acid (ABA)
CC (PubMed:19322584). First transiently repressed (1 day after treatment)
CC and later induced (2 days after treatment) by abscisic acid (ABA) and
CC dehydration (PubMed:25039074). {ECO:0000269|PubMed:19322584,
CC ECO:0000269|PubMed:25039074}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; EU183406; ABX38720.1; -; mRNA.
DR RefSeq; NP_001234517.1; NM_001247588.2.
DR AlphaFoldDB; A9QNE7; -.
DR SMR; A9QNE7; -.
DR STRING; 4081.Solyc04g078900.2.1; -.
DR PaxDb; A9QNE7; -.
DR PRIDE; A9QNE7; -.
DR EnsemblPlants; Solyc04g078900.3.1; Solyc04g078900.3.1; Solyc04g078900.3.
DR GeneID; 100136887; -.
DR Gramene; Solyc04g078900.3.1; Solyc04g078900.3.1; Solyc04g078900.3.
DR KEGG; sly:100136887; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_15_5_1; -.
DR OMA; AICQSNE; -.
DR OrthoDB; 871849at2759; -.
DR PhylomeDB; A9QNE7; -.
DR BRENDA; 1.14.14.137; 3101.
DR UniPathway; UPA00093; -.
DR Proteomes; UP000004994; Chromosome 4.
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:0046345; P:abscisic acid catabolic process; IMP:UniProtKB.
DR GO; GO:0009856; P:pollination; IEP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009733; P:response to auxin; 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..476
FT /note="Abscisic acid 8'-hydroxylase CYP707A1"
FT /id="PRO_0000445689"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 422
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 476 AA; 54337 MW; FE162068DD7651D6 CRC64;
MVNYFEIFLY ISMFVLGYLS YYFCFGKNNN SSSKKNAYKL PPGSMGWPYI GETLQLYSQD
PNAFFINRQR RFGEIFKTKI LGCPCVMLAS PEAARFVLVN QANLFKPTYP KSKENLIGQS
AIFFHQGDYH NHLRKLVQAP LNPESIRNQI PYIEELSISA LNSWVGGHVV NTYHEMKKFS
FEVGILAIFG HLDGHVKEEL KKNYSIVDKG YNSFPINLPG TLYRKALQAR KKLGKILSEI
IREMKEKKTL EKGLLSCFLN AKEEKGFLVL NEDQIADNII GVLFAAQDTT ASVLTWIIKY
LHDNPKLLEC VKAEQKVIWQ SNEQENHGLT WTQTRKMPIT SRVVLETLRM ASIISFAFRE
AVADVEYKGY LIPKGWKVMP LFRNIHHNPE FFPDPQKFDP SRFENAPKPN TFMPFGSGVH
ACPGNELAKL EILIMTHHLV TKFRWEVVGS GSGIQYGPFP VPLGGLAARF WKTTST
