ID   ZEP_ORYSJ               Reviewed;         659 AA.
AC   Q0JCU7; A0A0P0WB86; Q7XV26; Q9AVE7;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Zeaxanthin epoxidase, chloroplastic;
DE            Short=OsZEP1;
DE            EC=1.14.15.21;
DE   AltName: Full=Protein ABA DEFICIENT 1;
DE            Short=OsABA1;
DE   Flags: Precursor;
GN   Name=ZEP; Synonyms=ABA1; OrderedLocusNames=Os04g0448900, LOC_Os04g37619;
GN   ORFNames=OSJNBa0064H22.16;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11244106; DOI=10.1104/pp.125.3.1248;
RA   Agrawal G.K., Yamazaki M., Kobayashi M., Hirochika R., Miyao A.,
RA   Hirochika H.;
RT   "Screening of the rice viviparous mutants generated by endogenous
RT   retrotransposon Tos17 insertion. Tagging of a zeaxanthin epoxidase gene and
RT   a novel ostatc gene.";
RL   Plant Physiol. 125:1248-1257(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447439; DOI=10.1038/nature01183;
RA   Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA   Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA   Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA   Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA   Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA   Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA   Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA   Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA   Li J., Hong G., Xue Y., Han B.;
RT   "Sequence and analysis of rice chromosome 4.";
RL   Nature 420:316-320(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [6]
RP   TISSUE SPECIFICITY, AND INDUCTION BY COLD.
RX   PubMed=17693452; DOI=10.1093/pcp/pcm100;
RA   Oliver S.N., Dennis E.S., Dolferus R.;
RT   "ABA regulates apoplastic sugar transport and is a potential signal for
RT   cold-induced pollen sterility in rice.";
RL   Plant Cell Physiol. 48:1319-1330(2007).
CC   -!- FUNCTION: Zeaxanthin epoxidase that plays an important role in the
CC       xanthophyll cycle and abscisic acid (ABA) biosynthesis. Converts
CC       zeaxanthin into antheraxanthin and subsequently violaxanthin. Required
CC       for resistance to osmotic and drought stresses, seed development and
CC       dormancy. {ECO:0000269|PubMed:11244106}.
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
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in young microspores.
CC       {ECO:0000269|PubMed:17693452}.
CC   -!- INDUCTION: By cold in microspores. {ECO:0000269|PubMed:17693452}.
CC   -!- DISRUPTION PHENOTYPE: Accumulation of endogenous zeaxanthin and reduced
CC       level of ABA. Wilty phenotype, increased water loss and premature seed
CC       germination. {ECO:0000269|PubMed:11244106}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB39765.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAD40867.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB050884; BAB39765.1; ALT_FRAME; mRNA.
DR   EMBL; AL606448; CAD40867.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008210; BAF14840.1; -; Genomic_DNA.
DR   EMBL; AP014960; BAS89435.1; -; Genomic_DNA.
DR   RefSeq; XP_015636352.1; XM_015780866.1.
DR   RefSeq; XP_015636353.1; XM_015780867.1.
DR   AlphaFoldDB; Q0JCU7; -.
DR   SMR; Q0JCU7; -.
DR   STRING; 4530.OS04T0448900-00; -.
DR   PaxDb; Q0JCU7; -.
DR   PRIDE; Q0JCU7; -.
DR   EnsemblPlants; Os04t0448900-00; Os04t0448900-00; Os04g0448900.
DR   GeneID; 4335984; -.
DR   Gramene; Os04t0448900-00; Os04t0448900-00; Os04g0448900.
DR   KEGG; osa:4335984; -.
DR   eggNOG; KOG2614; Eukaryota.
DR   HOGENOM; CLU_009665_16_1_1; -.
DR   InParanoid; Q0JCU7; -.
DR   OMA; SCKDGAF; -.
DR   OrthoDB; 521070at2759; -.
DR   PlantReactome; R-OSA-1119449; Carotenoid biosynthesis.
DR   UniPathway; UPA00090; -.
DR   Proteomes; UP000000763; Chromosome 4.
DR   Proteomes; UP000059680; Chromosome 4.
DR   Genevisible; Q0JCU7; OS.
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; IMP:UniProtKB.
DR   GO; GO:0009688; P:abscisic acid biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0050891; P:multicellular organismal water homeostasis; IMP:UniProtKB.
DR   GO; GO:0009414; P:response to water deprivation; IMP:UniProtKB.
DR   GO; GO:0016123; P:xanthophyll biosynthetic process; IMP:UniProtKB.
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; Membrane;
KW   Oxidoreductase; Plastid; Reference proteome; Stress response; Thylakoid;
KW   Transit peptide.
FT   TRANSIT         1..50
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           51..659
FT                   /note="Zeaxanthin epoxidase, chloroplastic"
FT                   /id="PRO_0000412073"
FT   DOMAIN          553..607
FT                   /note="FHA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT   BINDING         79..107
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   BINDING         357..370
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        134
FT                   /note="E -> A (in Ref. 1; BAB39765)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   659 AA;  71798 MW;  E9F78E61F1DB036B CRC64;
     MALLSATAPA KTRFSLFSHE EAQHPHPHAL SACCGGGASG KRQRARARVA AAMRPADAAA
     SVAQAASPGG GGEGTRRPRV LVAGGGIGGL VLALAARRKG YEVTVFERDM SAVRGEGQYR
     GPIQIQSNAL AALEAIDMSV AEEVMREGCV TGDRINGLVD GISGSWYIKF DTFTPAAERG
     LPVTRVISRM TLQQILARAV GDDAILNDSH VVDFIDDGNK VTAILEDGRK FEGDLLVGAD
     GIWSKVRKVL FGQSEATYSE YTCYTGIADF VPPDIDTVGY RVFLGHKQYF VSSDVGAGKM
     QWYAFHKEPA GGTDPENGKN KRLLEIFNGW CDNVVDLINA TDEEAILRRD IYDRPPTFNW
     GKGRVTLLGD SVHAMQPNLG QGGCMAIEDG YQLAVELEKS WQESAKSGTP MDIVSSLRRY
     EKERILRVSV IHGLARMAAI MATTYRPYLG VGLGPLSFLT KLRIPHPGRV GGRFFIKYGM
     PLMLSWVLGG NSTKLEGRPL SCRLSDKAND QLRRWFEDDD ALEQAMGGEW YLLPTSSGDS
     QPIRLIRDEK KSLSIGSRSD PSNSTASLAL PLPQISENHA TITCKNKAFY VTDNGSEHGT
     WITDNEGRRY RVPPNFPVRF HPSDAIEFGS DKKAVFRVKV LSTLPYESAR GGPQILQAA