ENOXC_FRAAN
ID ENOXC_FRAAN Reviewed; 323 AA.
AC Q941I0;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=2-methylene-furan-3-one reductase;
DE EC=1.3.1.105 {ECO:0000269|PubMed:16517758, ECO:0000269|PubMed:23589283};
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], PROTEIN SEQUENCE OF 4-8 AND 292-301, FUNCTION,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP DEVELOPMENTAL STAGE, INDUCTION BY AUXIN, TISSUE SPECIFICITY, AND SUBUNIT.
RC STRAIN=cv. Chandler;
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 X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 2-322 IN COMPLEX WITH SUBSTRATE,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=23589283; DOI=10.1074/jbc.m113.453852;
RA Schiefner A., Sinz Q., Neumaier I., Schwab W., Skerra A.;
RT "Structural basis for the enzymatic formation of the key strawberry flavor
RT compound 4-hydroxy-2,5-dimethyl-3(2H)-furanone.";
RL J. Biol. Chem. 288:16815-16826(2013).
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}.
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:23589283};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.1 mM for (2E)-2-ethylidene-4-hydroxy-5-methyl-3(2H)-furanone
CC (EDHMF) {ECO:0000269|PubMed:16517758, ECO:0000269|PubMed:23589283};
CC KM=361 uM for NADH {ECO:0000269|PubMed:16517758,
CC ECO:0000269|PubMed:23589283};
CC KM=325 uM for NADPH {ECO:0000269|PubMed:16517758,
CC ECO:0000269|PubMed:23589283};
CC KM=35 uM for 9,10-phenanthrene quinone {ECO:0000269|PubMed:16517758,
CC ECO:0000269|PubMed:23589283};
CC Vmax=56 nmol/sec/mg enzyme {ECO:0000269|PubMed:16517758,
CC ECO:0000269|PubMed:23589283};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:16517758,
CC ECO:0000269|PubMed:23589283};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:16517758, ECO:0000269|PubMed:23589283};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16517758,
CC ECO:0000269|PubMed:23589283}.
CC -!- TISSUE SPECIFICITY: Expressed in parenchyma tissues of red fruits. Not
CC found in vascular tissues. Also detected in the achenes.
CC {ECO:0000269|PubMed:16517758}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during ripening.
CC {ECO:0000269|PubMed:16517758}.
CC -!- INDUCTION: Down-regulated by auxin. {ECO:0000269|PubMed:16517758}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY048861; AAL06644.1; -; mRNA.
DR PDB; 4IDA; X-ray; 1.60 A; A=2-322.
DR PDB; 4IDB; X-ray; 1.55 A; A=2-322.
DR PDB; 4IDC; X-ray; 1.40 A; A=2-322.
DR PDB; 4IDD; X-ray; 1.50 A; A=2-322.
DR PDB; 4IDE; X-ray; 1.60 A; A=2-322.
DR PDB; 4IDF; X-ray; 1.55 A; A=2-321.
DR PDBsum; 4IDA; -.
DR PDBsum; 4IDB; -.
DR PDBsum; 4IDC; -.
DR PDBsum; 4IDD; -.
DR PDBsum; 4IDE; -.
DR PDBsum; 4IDF; -.
DR AlphaFoldDB; Q941I0; -.
DR SMR; Q941I0; -.
DR BRENDA; 1.3.1.105; 2320.
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 3D-structure; Direct protein sequencing; NAD; NADP; Oxidoreductase.
FT CHAIN 1..323
FT /note="2-methylene-furan-3-one reductase"
FT /id="PRO_0000428657"
FT BINDING 59
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23589283"
FT BINDING 174..175
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 197..200
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 216
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 254
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 265..267
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 312..313
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
SQ SEQUENCE 323 AA; 34296 MW; ECFB11FD9607AA96 CRC64;
MAAAPSESIP SVNKAWVYSE YGKTSDVLKF DPSVAVPEIK EDQVLIKVVA ASLNPVDFKR
ALGYFKDTDS PLPTIPGYDV AGVVVKVGSQ VTKFKVGDEV YGDLNETALV NPTRFGSLAE
YTAAYERVLA HKPKNLSFIE AASLPLAIET AHEGLERAEL SAGKSVLVLG GAGGVGTHII
QLAKHVFGAS KVAATASTKK LDLLRTLGAA DLAIDYTKEN FEDLPEKFDV VYDAVGETDK
AVKAVKEGGK VVTIVGPATP PAILFVLTSK GSVLEKLKPY LESGKVKPVL DPTSPYPFTK
VVEAFGYLES SRATGKVVVY PIP
