ID   ABA2_PRUAR              Reviewed;         661 AA.
AC   O81360;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Zeaxanthin epoxidase, chloroplastic;
DE            EC=1.14.15.21;
DE   AltName: Full=PA-ZE;
DE   Flags: Precursor;
OS   Prunus armeniaca (Apricot) (Armeniaca vulgaris).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=36596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Bergeron; TISSUE=Exocarp, and Mesocarp;
RA   Mbeguie-A-Mbeguie D., Fils-Lycaon B.R.;
RT   "Molecular cloning and nucleotide sequences of PA-ZE and PA-ZE2, two cDNAs
RT   from apricot fruit coding for a zeaxanthin epoxidase. Gene expression
RT   during fruit ripening.";
RL   (er) Plant Gene Register PGR00-004(2000).
CC   -!- FUNCTION: Converts zeaxanthin into antheraxanthin and subsequently
CC       violaxanthin. Involved in the epoxidation of zeaxanthin. {ECO:0000250}.
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; AF071888; AAC24582.1; -; mRNA.
DR   EMBL; AF159948; AAD42899.1; -; mRNA.
DR   AlphaFoldDB; O81360; -.
DR   SMR; O81360; -.
DR   UniPathway; UPA00090; -.
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   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; 1.
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; Transit peptide.
FT   TRANSIT         1..50
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           51..661
FT                   /note="Zeaxanthin epoxidase, chloroplastic"
FT                   /id="PRO_0000020612"
FT   DOMAIN          558..607
FT                   /note="FHA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT   BINDING         82..110
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   BINDING         360..373
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   661 AA;  72483 MW;  F04716677474070A CRC64;
     MASTLFYNSM NLSAAVFSRT HFPIPINKDF PLEFSPCIHT DYHLRSRTRS GQKKCLTEVR
     ATVASPTEVP SAPASTQPKK LRILVAGGGI GGLVFALAAK KKGFDVVVFE KDLSAVRGEG
     QYRGPIQIQS NALAALEAID MDVAEEVMRV GCVTGDRING LVDGVSGTWY VKFDTFTPAV
     ERGLPVTRVI SRIALQQILA RAVGEEIIIN DSNVVNFEDL GDKVNVILEN GQRYEGDMLV
     GADGIWSKVR KNLFGLNEAV YSGYTCYTGI ADFVPADINS VGYRVFLGHK QYFVSSDVGG
     GKMQWYAFHK ESPGGVDSPN GKKERLLKIF EGWCDNVIDL LLATEEDAIL RRDIYDRTPI
     LTWGKGHVTL LGDSVHAMQP NMGQGGCMAI EDGYQLALEL DKAWKKSSET GTPVDVASSL
     RSYENSRRLR VAIIHGMARM AALMASTYKA YLGVGLGPLS FLTKFRIPHP GRVGGRVFID
     KAMPLMLSWV LGGNSSKLEG RSPSCRLSDK ASDQLRNWFE DDDALERAID GEWYLIPCGQ
     DNDASQLICL NRDEKNPCII GSAPHGDVSG ISIAIPKPQV SEMHARISYK DGAFYLTDLR
     SEHGTWIADI EGKRYRVPPN FPARFRPSDA IEIGSQKVAF RVKVMKSSPG SVEKEGILQA
     A