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ABA2_CAPAN
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   03-AUG-2022, entry version 118.
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:MON-2601; -.
DR   UniPathway; UPA00090; -.
DR   Proteomes; UP000189700; Genome assembly.
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   GO; GO:0009408; P:response to heat; IEA:EnsemblPlants.
DR   GO; GO:0010114; P:response to red light; IEA:EnsemblPlants.
DR   GO; GO:0009414; P:response to water deprivation; IEA:EnsemblPlants.
DR   GO; GO:0016123; P:xanthophyll biosynthetic process; IEA:EnsemblPlants.
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   SUPFAM; SSF49879; SSF49879; 1.
DR   SUPFAM; SSF51905; SSF51905; 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
 
 
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