KYE1_KLULA
ID KYE1_KLULA Reviewed; 398 AA.
AC P40952; Q6CXE2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Enoate reductase 1;
DE AltName: Full=2-enoate reductase;
DE Short=ER;
DE EC=1.3.1.31;
DE AltName: Full=Old yellow enzyme 1;
GN Name=KYE1; OrderedLocusNames=KLLA0A09075g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=7597850; DOI=10.1002/yea.320110509;
RA Miranda M., Ramirez J., Guevara S., Ongay-Larios L., Pena A., Coria R.;
RT "Nucleotide sequence and chromosomal localization of the gene encoding the
RT Old Yellow Enzyme from Kluyveromyces lactis.";
RL Yeast 11:459-465(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [3]
RP CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX DOI=10.1002/adsc.200700074;
RA Chaparro-Riggers J.F., Rogers T.A., Vazquez-Figueroa E., Polizzi K.M.,
RA Bommarius A.S.;
RT "Comparison of three enoate reductases and their potential use for
RT biotransformations.";
RL Adv. Synth. Catal. 349:1521-1531(2007).
CC -!- FUNCTION: Enoate reductase with broad substrate specificity for
CC different alpha,beta-unsaturated carbonyl compounds. Prefers NADPH over
CC NADH as cofactor.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoate + NAD(+) = (2E)-2-butenoate + H(+) + NADH;
CC Xref=Rhea:RHEA:10200, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968,
CC ChEBI:CHEBI:35899, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.31;
CC Evidence={ECO:0000269|Ref.3};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC -!- SUBUNIT: Homodimer or heterodimer.
CC -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC family. {ECO:0000305}.
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DR EMBL; L37452; AAA98815.1; -; Genomic_DNA.
DR EMBL; CR382121; CAH02985.1; -; Genomic_DNA.
DR PIR; S55844; S55844.
DR RefSeq; XP_451397.1; XM_451397.1.
DR AlphaFoldDB; P40952; -.
DR SMR; P40952; -.
DR STRING; 28985.XP_451397.1; -.
DR EnsemblFungi; CAH02985; CAH02985; KLLA0_A09075g.
DR GeneID; 2896828; -.
DR KEGG; kla:KLLA0_A09075g; -.
DR eggNOG; KOG0134; Eukaryota.
DR HOGENOM; CLU_012153_0_0_1; -.
DR InParanoid; P40952; -.
DR OMA; WHVGRFS; -.
DR BRENDA; 1.3.1.31; 2825.
DR Proteomes; UP000000598; Chromosome A.
DR GO; GO:0047540; F:2-enoate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR InterPro; IPR045247; Oye-like.
DR PANTHER; PTHR22893; PTHR22893; 1.
DR Pfam; PF00724; Oxidored_FMN; 1.
PE 1: Evidence at protein level;
KW Flavoprotein; FMN; NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..398
FT /note="Enoate reductase 1"
FT /id="PRO_0000194476"
FT ACT_SITE 196
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 256
FT /note="G -> V (in Ref. 1; AAA98815)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 44780 MW; AA40CCC0C2BE6EC1 CRC64;
MSFMNFEPKP LADTDIFKPI KIGNTELKHR VVMPALTRMR ALHPGNVPNP DWAVEYYRQR
SQYPGTMIIT EGAFPSAQSG GYDNAPGVWS EEQLAQWRKI FKAIHDNKSF VWVQLWVLGR
QAFADNLARD GLRYDSASDE VYMGEDEKER AIRSNNPQHG ITKDEIKQYI RDYVDAAKKC
IDAGADGVEI HSANGYLLNQ FLDPISNKRT DEYGGSIENR ARFVLEVVDA VVDAVGAERT
SIRFSPYGVF GTMSGGSDPV LVAQFAYVLA ELEKRAKAGK RLAYVDLVEP RVTSPFQPEF
EGWYKGGTNE FVYSVWKGNV LRVGNYALDP DAAITDSKNP NTLIGYGRAF IANPDLVERL
EKGLPLNQYD RPSFYKMSAE GYIDYPTYEE AVAKGYKK
