ID   ABA2_NICPL              Reviewed;         663 AA.
AC   Q40412;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Zeaxanthin epoxidase, chloroplastic;
DE            EC=1.14.15.21;
DE   Flags: Precursor;
GN   Name=ABA2;
OS   Nicotiana plumbaginifolia (Leadwort-leaved tobacco) (Tex-Mex tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4092;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CHARACTERIZATION.
RC   STRAIN=cv. Viviani; TISSUE=Seedling;
RX   PubMed=8665840; DOI=10.1002/j.1460-2075.1996.tb00589.x;
RA   Marin E., Nussaume L., Quesada A., Gonneau M., Sotta B., Hugueney P.,
RA   Frey A., Marion-Poll A.;
RT   "Molecular identification of zeaxanthin epoxidase of Nicotiana
RT   plumbaginifolia, a gene involved in abscisic acid biosynthesis and
RT   corresponding to the ABA locus of Arabidopsis thaliana.";
RL   EMBO J. 15:2331-2342(1996).
RN   [2]
RP   CHARACTERIZATION, FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Viviani;
RX   PubMed=9808747; DOI=10.1104/pp.118.3.1021;
RA   Audran C., Borel C., Frey A., Sotta B., Meyer C., Simonneau T.,
RA   Marion-Poll A.;
RT   "Expression studies of the zeaxanthin epoxidase gene in Nicotiana
RT   plumbaginifolia.";
RL   Plant Physiol. 118:1021-1028(1998).
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. {ECO:0000269|PubMed:8665840, ECO:0000269|PubMed:9808747}.
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 membrane; Peripheral
CC       membrane protein. Plastid, chloroplast thylakoid membrane; Peripheral
CC       membrane protein.
CC   -!- TISSUE SPECIFICITY: Higher expression in leaves than in roots.
CC       {ECO:0000269|PubMed:9808747}.
CC   -!- INDUCTION: By drought stress; in roots. {ECO:0000269|PubMed:9808747}.
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DR   EMBL; X95732; CAA65048.1; -; mRNA.
DR   PIR; S69548; S69548.
DR   AlphaFoldDB; Q40412; -.
DR   SMR; Q40412; -.
DR   PRIDE; Q40412; -.
DR   BioCyc; MetaCyc:MON-2602; -.
DR   BRENDA; 1.14.15.21; 3640.
DR   UniPathway; UPA00090; -.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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; 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   1: Evidence at protein level;
KW   Abscisic acid biosynthesis; Chloroplast; FAD; Flavoprotein; Membrane;
KW   Oxidoreductase; Plastid; Stress response; Thylakoid; Transit peptide.
FT   TRANSIT         1..50
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           51..663
FT                   /note="Zeaxanthin epoxidase, chloroplastic"
FT                   /id="PRO_0000020611"
FT   DOMAIN          547..611
FT                   /note="FHA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT   BINDING         81..109
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   BINDING         359..372
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   663 AA;  72524 MW;  D8D8BB4E73A661BA CRC64;
     MYSTVFYTSV HPSTSAFSRK QLPLLISKDF PTELYHSLPC SRSLENGQIK KVKGVVKATI
     AEAPATIPPT DLKKVPQKKL KVLVAGGGIG GLVFALAAKK RGFDVLVFER DLSAIRGEGQ
     YRGPIQIQSN ALAALEAIDM DVAEDIMNAG CITGQRINGL VDGVSGNWYC KFDTFTPAVE
     RGLPVTRVIS RMTLQQNLAR AVGEDIIMNE SNVVNFEDDG EKVTVTLEDG QQYTGDLLVG
     ADGIRSKVRT NLFGPSDVTY SGYTCYTGIA DFVPADIETV GYRVFLGHKQ YFVSSDVGGG
     KMQWYAFHNE PAGGVDDPNG KKARLLKIFE GWCDNVIDLL VATDEDAILR RDIYDRPPTF
     SWGKGRVTLL GDSVHAMQPN LGQGGCMAIE DSYQLALELD KALSRSAESG TPVDIISSLR
     SYESSRKLRV GVIHGLARMA AIMASTYKAY LGVGLGPLSF LTKFRIPHPG RVGGRFFIDL
     GMPLMLSWVL GGNGEKLEGR IQHCRLSEKA NDQLRNWFED DDALERATDA EWLLLPAGNS
     NAALETLVLS RDENMPCNIG SVSHANIPGK SVVIPLPQVS EMHARISYKG GAFFVTDLRS
     EHGTWITDNE GRRYRASPNF PTRFHPSDII EFGSDKKAAF RVKVMKFPPK TAAKEERQAV
     GAA