ENOXE_FRAAN
ID ENOXE_FRAAN Reviewed; 322 AA.
AC Q84V25;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=2-methylene-furan-3-one reductase;
DE EC=1.3.1.105 {ECO:0000269|PubMed:16517758, ECO:0000269|PubMed:17636940};
DE AltName: Full=Enone oxidoreductase;
DE Short=FaEO;
DE AltName: Full=Quinone oxidoreductase;
DE Short=FaQR;
GN Name=EO; Synonyms=QR;
OS Fragaria ananassa (Strawberry) (Fragaria chiloensis x Fragaria virginiana).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Rosoideae; Potentilleae; Fragariinae;
OC Fragaria.
OX NCBI_TaxID=3747;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, DEVELOPMENTAL STAGE, INDUCTION
RP BY AUXIN, TISSUE SPECIFICITY, AND SUBUNIT.
RC STRAIN=cv. Elsanta;
RX PubMed=16517758; DOI=10.1105/tpc.105.039784;
RA Raab T., Lopez-Raez J.A., Klein D., Caballero J.L., Moyano E., Schwab W.,
RA Munoz-Blanco J.;
RT "FaQR, required for the biosynthesis of the strawberry flavor compound 4-
RT hydroxy-2,5-dimethyl-3(2H)-furanone, encodes an enone oxidoreductase.";
RL Plant Cell 18:1023-1037(2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17636940; DOI=10.1021/jf071055o;
RA Klein D., Fink B., Arold B., Eisenreich W., Schwab W.;
RT "Functional characterization of enone oxidoreductases from strawberry and
RT tomato fruit.";
RL J. Agric. Food Chem. 55:6705-6711(2007).
CC -!- FUNCTION: Enone oxidoreductase involved in the biosynthesis of 4-
CC hydroxy-2,5-dimethyl-3(2H)-furanone (HDMF or furaneol), the key flavor
CC compound in strawberries. Can use both NADH and NADPH as the electron
CC donor. {ECO:0000269|PubMed:16517758, ECO:0000269|PubMed:17636940}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxy-2,5-dimethyl-furan-3(2H)-one + NADP(+) = 4-hydroxy-
CC 5-methyl-2-methylenefuran-3(2H)-one + H(+) + NADPH;
CC Xref=Rhea:RHEA:39111, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:76245, ChEBI:CHEBI:76247;
CC EC=1.3.1.105; Evidence={ECO:0000269|PubMed:16517758,
CC ECO:0000269|PubMed:17636940};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.14 mM for (2E)-2-ethylidene-4-hydroxy-5-methyl-3(2H)-furanone
CC (EDHMF) {ECO:0000269|PubMed:16517758, ECO:0000269|PubMed:17636940};
CC KM=1.04 mM for (2E)-4-hydroxy-5-methyl-2-propylidene-3(2H)-furanone
CC (HMPDF) {ECO:0000269|PubMed:16517758, ECO:0000269|PubMed:17636940};
CC KM=0.82 mM for (2E)-2-butylidene-4-hydroxy-5-methyl- 3(2H)-furanone
CC (BDHMF) {ECO:0000269|PubMed:16517758, ECO:0000269|PubMed:17636940};
CC Note=kcat is 1.94 sec(-1) with EDHMF as substrate. kcat is 2.69 sec(-
CC 1) with HMPDF as substrate. kcat is 1.43 sec(-1) with BDHMF as
CC substrate.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16517758}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during ripening.
CC {ECO:0000269|PubMed:16517758}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:16517758}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily. {ECO:0000305}.
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DR EMBL; AY158836; AAO22131.1; -; Genomic_DNA.
DR AlphaFoldDB; Q84V25; -.
DR SMR; Q84V25; -.
DR PRIDE; Q84V25; -.
DR BioCyc; MetaCyc:MON-14068; -.
DR GO; GO:0102978; F:furaneol oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR044626; AOR-like.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR PANTHER; PTHR44573; PTHR44573; 1.
DR Pfam; PF08240; ADH_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 1: Evidence at protein level;
KW NAD; NADP; Oxidoreductase.
FT CHAIN 1..322
FT /note="2-methylene-furan-3-one reductase"
FT /id="PRO_0000428656"
FT BINDING 59
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 174..175
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 197..200
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 264..266
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 311..322
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 311..312
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 322 AA; 34226 MW; A3E31A0E5BF79238 CRC64;
MAAAPSESIP SVNKAWVYSE YGKTSDVLKF DPSVAVPEVK EDQVLIKVVA ASLNPVDFKR
ALGYFKDTDS PLPTVPGYDV AGVVVKVGSQ VTKFKVGDEV YGDLNEAALV NPTRFGSLAE
YTAADERVLA HKPKDLSFIE AASLPLAIET AYEGLERAEL SAGKSILVLG GAGGVGTHII
QLAKHVFGAS KVAATASTKK LDFLRTLGVD LAIDYTKENI EDLPEKFDVV YDAVGETDKA
VKAVKEGGKV VTIVGPATPP AIHFVLTSKG SVLEKLKPYL ESGKVKPVLD PTSPYPFTKL
VEAFGYLESS RATGKVVVYP IP
