ID D3KZ29_CITUN Unreviewed; 664 AA.
AC D3KZ29;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Zeaxanthin epoxidase, chloroplastic {ECO:0000256|ARBA:ARBA00015103, ECO:0000256|PIRNR:PIRNR036989};
DE EC=1.14.15.21 {ECO:0000256|ARBA:ARBA00012097, ECO:0000256|PIRNR:PIRNR036989};
GN Name=ZEP {ECO:0000313|EMBL:BAI79258.1};
OS Citrus unshiu (Satsuma mandarin) (Citrus nobilis var. unshiu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=55188 {ECO:0000313|EMBL:BAI79258.1};
RN [1] {ECO:0000313|EMBL:BAI79258.1}
RP NUCLEOTIDE SEQUENCE.
RA Sugiyama A., Ikoma Y., Fujii H., Shimada T., Endo T., Omura M.;
RT "Structure and expression levels of alleles of Citrus zeaxanthin epoxidase
RT genes.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts zeaxanthin into antheraxanthin and subsequently
CC violaxanthin. {ECO:0000256|PIRNR:PIRNR036989}.
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 Evidence={ECO:0000256|PIRNR:PIRNR036989};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Hormone biosynthesis. {ECO:0000256|ARBA:ARBA00004972}.
CC -!- PATHWAY: Plant hormone biosynthesis; abscisate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005134, ECO:0000256|PIRNR:PIRNR036989}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|PIRNR:PIRNR036989}.
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DR EMBL; AB548571; BAI79258.1; -; Genomic_DNA.
DR AlphaFoldDB; D3KZ29; -.
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-UniRule.
DR CDD; cd22702; FHA_ZEP-like; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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 PANTHER; PTHR46496; -; 1.
DR PANTHER; PTHR46496:SF1; ZEAXANTHIN EPOXIDASE, CHLOROPLASTIC; 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 SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 4: Predicted;
KW Abscisic acid biosynthesis {ECO:0000256|ARBA:ARBA00022865,
KW ECO:0000256|PIRNR:PIRNR036989};
KW Chloroplast {ECO:0000256|ARBA:ARBA00022528, ECO:0000256|PIRNR:PIRNR036989};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR036989};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR036989};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR036989};
KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000256|PIRNR:PIRNR036989};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 556..610
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT REGION 50..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 664 AA; 73160 MW; 522FA3867F9DA52D CRC64;
MVSSMFYNSV NLSTAVFSRT HFPVPVYKHS CIEFSRYDHC INYKFRTGTS GQSKNPTQMK
AAVAESPTNN SDSENKKLRI LVAGGGIGGL VFALAAKRKG FEVLVFEKDM SAIRGEGQYR
GPIQIQSNAL AALEAIDLDV AEEVMRAGCV TGDRINGLVD GISGSWYIKF DTFTPAAEKG
LPVTRVISRM TLQQILAKAV GDEIILNESN VIDFKDHGDK VSVVLENGQC YAGDLLIGAD
GIWSKVRKNL FGPQEAIYSG YTCYTGIADF VPADIESVGY RVFLGHKQYF VSSDVGAGKM
QWYAFHKEPA GGVDGPEGKK ERLLKIFEGW CDNVVDLILA TDEEAILRRD IYDRTPIFTW
GRGRVTLLGD SVHAMQPNLG QGGCMAIEDG YQLAVELEKA CKKSNESKTP IDIVSALKSY
ERARRLRVAV IHGLARSAAV MASTYKAYLG VGLGPLSFLT KFRIPHPGRV GGRFFIDLAM
PLMLSWVLGG NSSKLKVGHR VASSRTKASD NLRTWFRDDD ALERAMNGEW FLVPSGSENV
VSQPIYLSGS HENEPYLIGS ESHEDFPRTS IVIPSAQVSK MHARISYKDG AFYLIDLQSE
HGTYVTDNEG RRYRVSSNFP ARFRPSDTIE FGSDKKAIFR VKVIGTPPNN NSERKEAGEI
LQAV
//
