ENOX_SOLLC
ID ENOX_SOLLC Reviewed; 388 AA.
AC K4BW79;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=2-methylene-furan-3-one reductase;
DE EC=1.3.1.105 {ECO:0000269|PubMed:16517758};
DE AltName: Full=Enone oxidoreductase;
DE Short=SlEO;
DE Flags: Precursor;
GN Name=EO; Synonyms=QR; OrderedLocusNames=Solyc05g005480;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [2]
RP IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBSTRATE SPECIFICITY.
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).
CC -!- FUNCTION: Enone oxidoreductase involved in the biosynthesis of 4-
CC hydroxy-2,5-dimethyl-3(2H)-furanone (HDMF or furaneol). Can use both
CC NADH and NADPH as the electron donor. {ECO:0000269|PubMed:16517758}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.59 mM for (2E)-2-ethylidene-4-hydroxy-5-methyl-3(2H)-furanone
CC (EDHMF) {ECO:0000269|PubMed:16517758};
CC KM=2.41 mM for (2E)-4-hydroxy-5-methyl-2-propylidene-3(2H)-furanone
CC (HMPDF) {ECO:0000269|PubMed:16517758};
CC KM=1.13 mM for (2E)-2-butylidene-4-hydroxy-5-methyl- 3(2H)-furanone
CC (BDHMF) {ECO:0000269|PubMed:16517758};
CC Note=kcat is 0.39 sec(-1) with EDHMF as substrate. kcat is 0.34 sec(-
CC 1) with HMPDF as substrate. kcat is 0.15 sec(-1) with BDHMF as
CC substrate.;
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily. {ECO:0000305}.
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DR RefSeq; NP_001296292.1; NM_001309363.1.
DR AlphaFoldDB; K4BW79; -.
DR SMR; K4BW79; -.
DR STRING; 4081.Solyc05g005480.2.1; -.
DR PaxDb; K4BW79; -.
DR PRIDE; K4BW79; -.
DR GeneID; 101250690; -.
DR KEGG; sly:101250690; -.
DR eggNOG; KOG1198; Eukaryota.
DR HOGENOM; CLU_026673_3_3_1; -.
DR InParanoid; K4BW79; -.
DR OrthoDB; 727365at2759; -.
DR PhylomeDB; K4BW79; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; K4BW79; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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 Chloroplast; NAD; NADP; Oxidoreductase; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..60
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 61..388
FT /note="2-methylene-furan-3-one reductase"
FT /id="PRO_0000428658"
FT BINDING 125
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 240..241
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 263..266
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 330..332
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 377..378
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 388 AA; 41001 MW; 8B771021B868D85C CRC64;
MEALLSSTTL QLKPLHPPSS FSSLHSPFSS ISVLRVKGSK KAETFIQRSN FSTVLPLRVS
ASSQAAAAET STSISIPSEM KAWSYTDYGS VDVLKLESNV AVPDIKEDQV LIKIVAAALN
PVDFKRRLGK FKATDSPLPT VPGYDVAGVV VKVGSQVKGL KEGDEVYGDI HEKALDGPKQ
FGSLAEYTAV EEKLVALKPK NLSFAEAAAL PLAIETAYEG LEKAGFSSGK SILVLGGAGG
VGSLVIQLAK HVFGASKVAA TSSTGKLELL KSLGADLAID YTKENFEDLP DKFDVVYDSV
GQGEKAVKVV KEGGSVVVLT GAVTPPGFRF VVTSNGEMLK KLNPYLESGK VKPVIDPKGP
FSFDKVVDAF SYLETGRATG KVVIHPIP
