ID   ABA2_SOLLC              Reviewed;         669 AA.
AC   P93236;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Zeaxanthin epoxidase, chloroplastic;
DE            EC=1.14.15.21;
DE   Flags: Precursor;
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].
RA   Burbidge A., Grieve T., Terry C., Corlett J., Thompson A., Taylor I.;
RT   "Structure and expression of a cDNA encoding zeaxanthine epoxidase,
RT   isolated from a wilt-related tomato (Lycopersicon esculentum Mill.)
RT   library.";
RL   J. Exp. Bot. 48:1749-1750(1997).
CC   -!- FUNCTION: Converts zeaxanthin into antheraxanthin and subsequently
CC       violaxanthin. Involved in the epoxidation of zeaxanthin. Plays an
CC       important role in resistance to stresses, seed development and
CC       dormancy.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-zeaxanthin + 4 H(+) + 2 O2 + 4 reduced [2Fe-2S]-
CC         [ferredoxin] = all-trans-violaxanthin + 2 H2O + 4 oxidized [2Fe-2S]-
CC         [ferredoxin]; Xref=Rhea:RHEA:32443, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC         COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:27547, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:35288; EC=1.14.15.21;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- PATHWAY: Plant hormone biosynthesis; abscisate biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
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DR   EMBL; Z83835; CAB06084.1; -; mRNA.
DR   PIR; T07754; T07754.
DR   AlphaFoldDB; P93236; -.
DR   SMR; P93236; -.
DR   STRING; 4081.Solyc02g090890.2.1; -.
DR   PaxDb; P93236; -.
DR   PRIDE; P93236; -.
DR   eggNOG; KOG2614; Eukaryota.
DR   BRENDA; 1.14.15.21; 3101.
DR   UniPathway; UPA00090; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; P93236; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0052662; F:zeaxanthin epoxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009688; P:abscisic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009408; P:response to heat; IEA:EnsemblPlants.
DR   GO; GO:0010114; P:response to red light; IEA:EnsemblPlants.
DR   GO; GO:0009414; P:response to water deprivation; IEA:EnsemblPlants.
DR   GO; GO:0016123; P:xanthophyll biosynthetic process; IEA:EnsemblPlants.
DR   CDD; cd00060; FHA; 1.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   InterPro; IPR017079; Zeaxanthin_epoxidase.
DR   Pfam; PF01494; FAD_binding_3; 2.
DR   Pfam; PF00498; FHA; 1.
DR   PIRSF; PIRSF036989; Zeaxanthin_epoxidase; 1.
DR   SMART; SM00240; FHA; 1.
DR   SUPFAM; SSF49879; SSF49879; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Abscisic acid biosynthesis; Chloroplast; FAD; Flavoprotein; Oxidoreductase;
KW   Plastid; Reference proteome; Transit peptide.
FT   TRANSIT         1..49
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           50..669
FT                   /note="Zeaxanthin epoxidase, chloroplastic"
FT                   /id="PRO_0000020610"
FT   DOMAIN          553..617
FT                   /note="FHA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT   BINDING         87..115
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   BINDING         365..378
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   669 AA;  73102 MW;  1140C9F29C3499B7 CRC64;
     MYSTVFYTSV HPSTSVLSRK QLPLLISKDF SAELYHSLPC RSLENGHINK VKGVKVKATI
     AEAPVTPTEK TDSGANGDLK VPQKKLKVLV AGGGIGGLVF ALAAKKRGFD VLVFERDLSA
     IRGEGQYRGP IQIQSNALAA LEAIDLDVAE DIMNAGCITG QRINGLVDGI SGNWYCKFDT
     FTPAVERGLP VTRVISRMTL QQILARAVGE EIIMNESNVV DFEDDGEKVT VVLENGQRFT
     GDLLVGADGI RSKVRTNLFG PSEATYSGYT CYTGIADFVP ADIDTVGYRV FLGHKQYFVS
     SDVGGGKMQW YAFYNEPAGG ADAPNGKKER LLKIFGGWCD NVIDLLVATD EDAILRRDIY
     DRPPTFSWGR GRVTLLGDSV HAMQPNLGQG GCMAIEDSYQ LALELEKACS RSAEFGSPVD
     IISSLRSYES ARKLRVGVIH GLARMAAIMA STYKAYLGVG LGPLSFLTQY RIPHPGRVGG
     RVFIDLGMPL MLSWVLGGNG DKLEGRIKHC RLSEKANDQL RKWFEDDDAL ERATDAEWLL
     LPAGNGSSGL EAIVLSRDED VPCTVGSISH TNIPGKSIVL PLPQVSEMHA RISCKDGAFF
     VTDLRSEHGT WVTDNEGRRY RTSPNFPTRF HPSDVIEFGS DKAAFRVKAM KFPLKTSERK
     EEREAVEAA