ABA2_SPIOL
ID ABA2_SPIOL Reviewed; 675 AA.
AC A0A0K9RDW0;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Zeaxanthin epoxidase, chloroplastic {ECO:0000255|PIRNR:PIRNR036989};
DE EC=1.14.15.21 {ECO:0000269|PubMed:8521963};
DE Flags: Precursor;
GN ORFNames=SOVF_077800 {ECO:0000312|EMBL:KNA17670.1};
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Viroflay; TISSUE=Leaf;
RX PubMed=24352233; DOI=10.1038/nature12817;
RA Dohm J.C., Minoche A.E., Holtgraewe D., Capella-Gutierrez S.,
RA Zakrzewski F., Tafer H., Rupp O., Soerensen T.R., Stracke R., Reinhardt R.,
RA Goesmann A., Kraft T., Schulz B., Stadler P.F., Schmidt T., Gabaldon T.,
RA Lehrach H., Weisshaar B., Himmelbauer H.;
RT "The genome of the recently domesticated crop plant sugar beet (Beta
RT vulgaris).";
RL Nature 505:546-549(2014).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, AND ACTIVITY
RP REGULATION.
RC STRAIN=cv. Butterfly;
RX PubMed=8521963; DOI=10.1016/0014-5793(95)01243-9;
RA Buech K., Stransky H., Hager A.;
RT "FAD is a further essential cofactor of the NAD(P)H and O2-dependent
RT zeaxanthin-epoxidase.";
RL FEBS Lett. 376:45-48(1995).
CC -!- FUNCTION: Converts zeaxanthin into antheraxanthin and subsequently
CC violaxanthin. Involved in the epoxidation of zeaxanthin.
CC {ECO:0000269|PubMed:8521963}.
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:8521963};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:8521963};
CC Note=FAD enhances the epoxidase activity while other flavins such as
CC FMN or riboflavin are without effects. {ECO:0000269|PubMed:8521963};
CC -!- ACTIVITY REGULATION: Inhibited by diphenyleneiodonium (DPI).
CC {ECO:0000269|PubMed:8521963}.
CC -!- PATHWAY: Plant hormone biosynthesis; abscisate biosynthesis.
CC {ECO:0000255|PIRNR:PIRNR036989}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:8521963}.
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DR EMBL; KQ143372; KNA17670.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9RDW0; -.
DR SMR; A0A0K9RDW0; -.
DR STRING; 3562.A0A0K9RDW0; -.
DR OrthoDB; 521070at2759; -.
DR UniPathway; UPA00090; -.
DR Proteomes; UP000054095; Unassembled WGS sequence.
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; 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 1: Evidence at protein level;
KW Abscisic acid biosynthesis; Chloroplast; FAD; Flavoprotein; Membrane;
KW Oxidoreductase; Plastid; Reference proteome; Thylakoid; Transit peptide.
FT TRANSIT 1..25
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 26..675
FT /note="Zeaxanthin epoxidase, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000439082"
FT DOMAIN 558..622
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT BINDING 92..120
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 370..383
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 675 AA; 73576 MW; 25678E29FF2338E9 CRC64;
MASTVLYNSL TTSTTVFLRS HLPISSSSPN DELHHQSSVI SNCNYYLKKS SFGGQRKKLK
ENNNYVKAAA VAESLKTYPN EVAGDVPEKK LRILVAGGGI GGLVFALAAK KRGFDVKVFE
KDLSAIRGEG KYRGPIQVQS NALAALEAID MDVAEKVLAA GCVTGDRING LVDGVSGNWY
VKFDTFTPAV ERGLPVTRVI SRMTLQQILA EAVGEEVITN ESNVVDFKDD GNKVSVTLDN
GKTFEGDLLV GADGIWSKVR TNLFGHSDAV YSGYTCYTGI ADYVPADIDS VGYRVFLGNK
QYFVSSDVGG GKMQWYAFYK EAPGGVDQPN GMKQRLFDIF EGWCDNVIDV IIATDEEAIL
RRDIYDRTPK LTWGQGRVTL LGDSVHAMQP NLGQGGCMAI EDSYELALTL DKAWQKSVES
GRPIDVASSL KSYEGARRLR VGVIHGLARL AAVMATTYKS YLGIGLGPLS FLTKLRIPHP
GRVGGRFFIT PAMPLMLRWI LGGNSEKLEG RIPYCSLSEK ASNNLQRWFE DDDALERALT
GEWTLLPQGS VAGSLKPICL SRKEDEPCII GGVFHKDSSG MSVALSSPQI SEKHAQITCK
NGAYFVTDLG SEHGTWITDN EGRNYRLPPN FPTRFHPSDV IEFGTDKKAV YRVKVMATPP
KASQNSPSAA VLQTA
