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   16-JUN-2009, entry version 64.
DE   RecName: Full=Zeaxanthin epoxidase, chloroplastic;
DE            EC=1.14.13.90;
DE   Flags: Precursor;
GN   Name=ABA2;
OS   Nicotiana plumbaginifolia (Leadwort-leaved tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4092;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC   STRAIN=cv. Viviani; TISSUE=Seedling;
RX   MEDLINE=96221293; PubMed=8665840;
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.
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.
CC   -!- CATALYTIC ACTIVITY: Zeaxanthin + NAD(P)H + O(2) = antheraxanthin +
CC       NAD(P)(+) + H(2)O.
CC   -!- CATALYTIC ACTIVITY: Antheraxanthin + NAD(P)H + O(2) = violaxanthin
CC       + NAD(P)(+) + H(2)O.
CC   -!- COFACTOR: FAD (Potential).
CC   -!- PATHWAY: Plant hormone biosynthesis; abscisic acid biosynthesis.
CC   -!- PATHWAY: Lipid metabolism; steroid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Peripheral
CC       membrane protein. Plastid, chloroplast thylakoid membrane;
CC       Peripheral membrane protein.
CC   -!- TISSUE SPECIFICITY: Higher expression in leaves than in roots.
CC   -!- INDUCTION: By drought stress; in roots.
CC   -!- SIMILARITY: Contains 1 FHA domain.
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DR   EMBL; X95732; CAA65048.1; -; mRNA.
DR   PIR; S69548; S69548.
DR   BioCyc; MetaCyc:MON-2602; -.
DR   BRENDA; 1.14.13.90; 257040.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009540; F:zeaxanthin epoxidase activity; IEA:EC.
DR   GO; GO:0009688; P:abscisic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   InterPro; IPR000253; FHA.
DR   InterPro; IPR002938; mOase_FAD_bd.
DR   InterPro; IPR003042; Rng_hydrolase-like.
DR   InterPro; IPR017079; Zeaxanthin_epoxidase.
DR   Gene3D; G3DSA:2.60.200.20; FHA; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   Pfam; PF00498; FHA; 1.
DR   PIRSF; PIRSF036989; Zeaxanthin_epoxidase; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SMART; SM00240; FHA; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Abscisic acid biosynthesis; Chloroplast; FAD; Flavoprotein; Membrane;
KW   NAD; NADP; Oxidoreductase; Plastid; Stress response; Transit peptide.
FT   TRANSIT       1     50       Chloroplast (Potential).
FT   CHAIN        51    663       Zeaxanthin epoxidase, chloroplastic.
FT                                /FTId=PRO_0000020611.
FT   DOMAIN      547    611       FHA.
FT   NP_BIND      81    109       FAD (Potential).
FT   NP_BIND     359    372       FAD (Potential).
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
//