ID ABA2_CAPAN Reviewed; 660 AA.
AC Q96375;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE RecName: Full=Zeaxanthin epoxidase, chloroplastic {ECO:0000303|PubMed:8910532};
DE EC=1.14.15.21 {ECO:0000269|PubMed:8910532};
DE AltName: Full=Beta-cyclohexenyl epoxidase {ECO:0000303|PubMed:8910532};
DE AltName: Full=Xanthophyll epoxidase {ECO:0000303|PubMed:8910532};
DE Flags: Precursor;
OS Capsicum annuum (Capsicum pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=4072;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP INDUCTION.
RC STRAIN=cv. Yolo Wonder;
RX PubMed=8910532; DOI=10.1074/jbc.271.46.28861;
RA Bouvier F., D'Harlingue A., Hugueney P., Marin E., Marion-Poll A.,
RA Camara B.;
RT "Xanthophyll biosynthesis. Cloning, expression, functional reconstitution,
RT and regulation of beta-cyclohexenyl carotenoid epoxidase from pepper
RT (Capsicum annuum).";
RL J. Biol. Chem. 271:28861-28867(1996).
CC -!- FUNCTION: Converts zeaxanthin into antheraxanthin and subsequently
CC violaxanthin. Acts also on beta-cryptoxanthin. Involved in the
CC epoxidation of zeaxanthin. {ECO:0000269|PubMed:8910532}.
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:0000269|PubMed:8910532};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32444;
CC Evidence={ECO:0000269|PubMed:8910532};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-zeaxanthin + 2 H(+) + O2 + 2 reduced [2Fe-2S]-
CC [ferredoxin] = all-trans-antheraxanthin + H2O + 2 oxidized [2Fe-2S]-
CC [ferredoxin]; Xref=Rhea:RHEA:24084, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:27547, ChEBI:CHEBI:27867, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738; Evidence={ECO:0000269|PubMed:8910532};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24085;
CC Evidence={ECO:0000269|PubMed:8910532};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-antheraxanthin + 2 H(+) + O2 + 2 reduced [2Fe-2S]-
CC [ferredoxin] = all-trans-violaxanthin + H2O + 2 oxidized [2Fe-2S]-
CC [ferredoxin]; Xref=Rhea:RHEA:14937, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:27867, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:35288; Evidence={ECO:0000269|PubMed:8910532};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14938;
CC Evidence={ECO:0000269|PubMed:8910532};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-cryptoxanthin + 2 H(+) + O2 + 2 reduced [2Fe-2S]-
CC [ferredoxin] = (5R,6S)-5,6-epoxi-beta-cryptoxanthin + H2O + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:49316, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:10362,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:91143;
CC Evidence={ECO:0000269|PubMed:8910532};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49317;
CC Evidence={ECO:0000269|PubMed:8910532};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:8910532};
CC -!- PATHWAY: Plant hormone biosynthesis; abscisate biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Peripheral
CC membrane protein. Plastid, chloroplast thylakoid membrane; Peripheral
CC membrane protein.
CC -!- INDUCTION: Up-regulated by oxidative stress and when chloroplasts
CC undergo differentiation into chromoplasts.
CC {ECO:0000269|PubMed:8910532}.
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DR EMBL; X91491; CAA62795.1; -; mRNA.
DR PIR; T09537; T09537.
DR AlphaFoldDB; Q96375; -.
DR SMR; Q96375; -.
DR SwissLipids; SLP:000001507; -.
DR BioCyc; MetaCyc:MONOMER-2601; -.
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; 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 SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
PE 1: Evidence at protein level;
KW Abscisic acid biosynthesis; Chloroplast; FAD; Flavoprotein; Membrane;
KW Oxidoreductase; Plastid; Thylakoid; Transit peptide.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..660
FT /note="Zeaxanthin epoxidase, chloroplastic"
FT /id="PRO_0000020609"
FT DOMAIN 545..609
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"
SQ SEQUENCE 660 AA; 71952 MW; 80AF5D8F7D381121 CRC64;
MYASSARDGI PGKWCNARRK QLPLLISKDF PAELYHSLPC KSLENGHIKK VKGVKATLAE
APATPTEKSN SEVPQKKLKV LVAGGGIGGL VFALAGKKRG FDVLVFERDI SAIRGEGQYR
GPIQIQSNAL AALEAIDMDV AEEIMNAGCI TGQRINGLVD GISGNWYCKF DTFTPAVERG
LPVTRVISRM TLQQILARLQ GEDVIMNESH VVNFADDGET VTVNPELCQQ YTGDLLVGAD
GIRSKVRTNL FGPSELTYSG YTCYTGIADF VPADIDTAGY RVFLGHKQYF VSSDVGGGKM
QWYAFHNEPA GGVDAPNGKK ERLLKIFGGW CDNVIDLSVA TDEDAILRRD IYDRPPTFSW
GKGRVTLLGD SVHAMQPNLG QGGCMAIEDS YQLALELEKA WSRSAESGSP MDVISSLRSY
ESARKLRVGV IHGLARMAAI MASAYKAYLG VGLGPLSFIT KFRIPHPGRV GGRFFIDLGM
PLMLSWVLGG NGEKLEGRIQ HCRLSEKAND QLRNWFEDDD ALERATDAEW LLLPAGNSNA
ALETLVLSRD ENMPCTIGSV SHANIPGKSV VIPLSQVSDM HARISYNGGA FLGTAFRSDH
GTWFIDNEGR RYRVSPNFPM RFHSSDVIVF GSDKAAFRIK AMKFAPKTAA KEDRQAVGAA
//
