OYE1_SACPS
ID OYE1_SACPS Reviewed; 400 AA.
AC Q02899;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=NADPH dehydrogenase 1 {ECO:0000303|PubMed:1939123};
DE EC=1.6.99.1 {ECO:0000305|PubMed:8454584};
DE AltName: Full=Old yellow enzyme 1 {ECO:0000303|PubMed:1939123};
GN Name=OYE1 {ECO:0000303|PubMed:1939123};
OS Saccharomyces pastorianus (Lager yeast) (Saccharomyces cerevisiae x
OS Saccharomyces eubayanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=27292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-47.
RC STRAIN=Brewer's bottom;
RX PubMed=1939123; DOI=10.1016/s0021-9258(18)54768-2;
RA Saito K., Thiele D.J., Davio M., Lockridge O., Massey V.;
RT "The cloning and expression of a gene encoding Old Yellow Enzyme from
RT Saccharomyces carlsbergensis.";
RL J. Biol. Chem. 266:20720-20724(1991).
RN [2]
RP PROTEIN SEQUENCE OF 2-37, CLEAVAGE OF INITIATOR METHIONINE, AND MASS
RP SPECTROMETRY.
RX PubMed=8454584; DOI=10.1016/s0021-9258(18)53224-5;
RA Stott K., Saito K., Thiels D.J., Massey V.;
RT "Old Yellow Enzyme. The discovery of multiple isozymes and a family of
RT related proteins.";
RL J. Biol. Chem. 268:6097-6106(1993).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=3944085; DOI=10.1016/s0021-9258(17)36078-7;
RA Massey V., Schopfer L.M.;
RT "Reactivity of old yellow enzyme with alpha-NADPH and other pyridine
RT nucleotide derivatives.";
RL J. Biol. Chem. 261:1215-1222(1986).
RN [4]
RP MASS SPECTROMETRY.
RX PubMed=7836424; DOI=10.1074/jbc.270.5.1983;
RA Niino Y.S., Chakraborty S., Brown B.J., Massey V.;
RT "A new old yellow enzyme of Saccharomyces cerevisiae.";
RL J. Biol. Chem. 270:1983-1991(1995).
RN [5]
RP ACTIVE SITE, AND MUTAGENESIS OF TYR-197.
RX PubMed=9830020; DOI=10.1074/jbc.273.49.32763;
RA Kohli R.M., Massey V.;
RT "The oxidative half-reaction of Old Yellow Enzyme. The role of tyrosine
RT 196.";
RL J. Biol. Chem. 273:32763-32770(1998).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH FMN AND SUBSTRATE.
RX PubMed=7881908; DOI=10.1016/s0969-2126(94)00111-1;
RA Fox K.M., Karplus P.A.;
RT "Old yellow enzyme at 2-A resolution: overall structure, ligand binding,
RT and comparison with related flavoproteins.";
RL Structure 2:1089-1105(1994).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH FMN, MUTAGENESIS OF
RP HIS-192, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9830019; DOI=10.1074/jbc.273.49.32753;
RA Brown B.J., Deng Z., Karplus P.A., Massey V.;
RT "On the active site of Old Yellow Enzyme. Role of histidine 191 and
RT asparagine 194.";
RL J. Biol. Chem. 273:32753-32762(1998).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF MUTANT ASN-115 IN COMPLEX WITH FMN
RP AND SUBSTRATE.
RX PubMed=11668181; DOI=10.1074/jbc.m108453200;
RA Brown B.J., Hyun J.-W., Duvvuri S., Karplus P.A., Massey V.;
RT "The role of glutamine 114 in Old Yellow Enzyme.";
RL J. Biol. Chem. 277:2138-2145(2002).
CC -!- FUNCTION: Flavin-dependent enoate reductase that catalyzes the
CC chemo- and stereoslective hydrogenation of electron-poor alkenes. The
CC enzyme is reduced by NADPH, and oxygen, quinones, and alpha,beta-
CC unsaturated aldehydes and ketones can act as electron acceptors to
CC complete catalytic turnover. The physiological oxidant remains elusive.
CC {ECO:0000269|PubMed:3944085, ECO:0000269|PubMed:9830019}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + H(+) + NADPH = AH2 + NADP(+); Xref=Rhea:RHEA:13149,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.99.1;
CC Evidence={ECO:0000269|PubMed:9830019, ECO:0000305|PubMed:8454584};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:11668181, ECO:0000269|PubMed:7881908,
CC ECO:0000269|PubMed:9830019, ECO:0000305|PubMed:8454584};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11.4 uM for alpha-NADPH {ECO:0000269|PubMed:3944085};
CC KM=7.7 uM for beta-NADPH {ECO:0000269|PubMed:3944085};
CC KM=1.18 mM for oxygen (with alpha-NADPH a substrate)
CC {ECO:0000269|PubMed:3944085};
CC KM=0.88 mM for oxygen (with beta-NADPH a substrate)
CC {ECO:0000269|PubMed:3944085};
CC -!- SUBUNIT: Homodimer or heterodimer. {ECO:0000269|PubMed:11668181,
CC ECO:0000269|PubMed:7881908, ECO:0000269|PubMed:9830019}.
CC -!- MASS SPECTROMETRY: Mass=44890; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:7836424, ECO:0000269|PubMed:8454584};
CC -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC family. {ECO:0000305}.
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DR EMBL; X53597; CAA37666.1; -; Genomic_DNA.
DR PIR; A39495; A39495.
DR PDB; 1BWK; X-ray; 2.30 A; A=2-399.
DR PDB; 1BWL; X-ray; 2.70 A; A=2-399.
DR PDB; 1K02; X-ray; 2.70 A; A=2-400.
DR PDB; 1K03; X-ray; 2.70 A; A=2-400.
DR PDB; 1OYA; X-ray; 2.00 A; A=1-400.
DR PDB; 1OYB; X-ray; 2.00 A; A=1-400.
DR PDB; 1OYC; X-ray; 2.00 A; A=1-400.
DR PDB; 3RND; X-ray; 1.40 A; A=2-400.
DR PDB; 3TX9; X-ray; 2.00 A; A=1-400.
DR PDB; 3TXZ; X-ray; 1.70 A; A=1-400.
DR PDB; 4GBU; X-ray; 1.18 A; A=1-400.
DR PDB; 4GE8; X-ray; 1.50 A; A=1-400.
DR PDB; 4GWE; X-ray; 1.45 A; A=1-400.
DR PDB; 4GXM; X-ray; 1.36 A; A=1-400.
DR PDB; 4H4I; X-ray; 1.25 A; A=1-400.
DR PDB; 4H6K; X-ray; 1.55 A; A=2-400.
DR PDB; 4K7V; X-ray; 1.52 A; A=1-400.
DR PDB; 4K7Y; X-ray; 1.20 A; A=1-400.
DR PDB; 4K8E; X-ray; 1.27 A; A=1-400.
DR PDB; 4K8H; X-ray; 1.55 A; A=1-400.
DR PDB; 4RNU; X-ray; 2.68 A; A/B/C/D=2-397.
DR PDB; 4RNV; X-ray; 2.47 A; A/B/C/D=2-397.
DR PDB; 4RNW; X-ray; 1.55 A; A/B=2-292, A/B=307-397.
DR PDB; 4RNX; X-ray; 1.25 A; A/B=2-397.
DR PDB; 4YIL; X-ray; 1.46 A; A=2-398.
DR PDB; 4YNC; X-ray; 1.50 A; A=2-398.
DR PDBsum; 1BWK; -.
DR PDBsum; 1BWL; -.
DR PDBsum; 1K02; -.
DR PDBsum; 1K03; -.
DR PDBsum; 1OYA; -.
DR PDBsum; 1OYB; -.
DR PDBsum; 1OYC; -.
DR PDBsum; 3RND; -.
DR PDBsum; 3TX9; -.
DR PDBsum; 3TXZ; -.
DR PDBsum; 4GBU; -.
DR PDBsum; 4GE8; -.
DR PDBsum; 4GWE; -.
DR PDBsum; 4GXM; -.
DR PDBsum; 4H4I; -.
DR PDBsum; 4H6K; -.
DR PDBsum; 4K7V; -.
DR PDBsum; 4K7Y; -.
DR PDBsum; 4K8E; -.
DR PDBsum; 4K8H; -.
DR PDBsum; 4RNU; -.
DR PDBsum; 4RNV; -.
DR PDBsum; 4RNW; -.
DR PDBsum; 4RNX; -.
DR PDBsum; 4YIL; -.
DR PDBsum; 4YNC; -.
DR AlphaFoldDB; Q02899; -.
DR SMR; Q02899; -.
DR EvolutionaryTrace; Q02899; -.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0003959; F:NADPH dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0018548; F:pentaerythritol trinitrate reductase activity; IEA:UniProtKB-EC.
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 3D-structure; Direct protein sequencing; Flavoprotein; FMN; NADP;
KW Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1939123"
FT CHAIN 2..400
FT /note="NADPH dehydrogenase 1"
FT /id="PRO_0000194473"
FT ACT_SITE 197
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:9830020"
FT BINDING 38
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:11668181,
FT ECO:0000269|PubMed:7881908, ECO:0000269|PubMed:9830019"
FT BINDING 115
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:11668181,
FT ECO:0000269|PubMed:7881908, ECO:0000269|PubMed:9830019"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11668181,
FT ECO:0000269|PubMed:7881908"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11668181,
FT ECO:0000269|PubMed:7881908"
FT BINDING 244
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:11668181,
FT ECO:0000269|PubMed:7881908, ECO:0000269|PubMed:9830019"
FT BINDING 349
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:11668181,
FT ECO:0000269|PubMed:7881908, ECO:0000269|PubMed:9830019"
FT BINDING 376
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11668181,
FT ECO:0000269|PubMed:7881908"
FT MUTAGEN 115
FT /note="Q->N: Strong reduction of substrate binding."
FT /evidence="ECO:0000269|PubMed:11668181"
FT MUTAGEN 192
FT /note="H->N: Strong reduction of substrate binding. Reduced
FT oxidation of NADPH."
FT /evidence="ECO:0000269|PubMed:9830019"
FT MUTAGEN 197
FT /note="Y->F: Reduces oxidative half-reaction with 2-
FT cyclohexenone 6-fold."
FT /evidence="ECO:0000269|PubMed:9830020"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:4RNU"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:4RNU"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:4GBU"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:4GBU"
FT STRAND 26..34
FT /evidence="ECO:0007829|PDB:4GBU"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:4GBU"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:4GBU"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:4GBU"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:4GBU"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:4GBU"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:4GBU"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:4GBU"
FT HELIX 92..107
FT /evidence="ECO:0007829|PDB:4GBU"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:4GBU"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:4GBU"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:4GBU"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:4GBU"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:4GE8"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:4GBU"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:4RNX"
FT HELIX 164..183
FT /evidence="ECO:0007829|PDB:4GBU"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:4GBU"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:4GBU"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:4GBU"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:4GBU"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:4GBU"
FT HELIX 223..236
FT /evidence="ECO:0007829|PDB:4GBU"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:4GBU"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:4GBU"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:4GBU"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:4GBU"
FT HELIX 262..278
FT /evidence="ECO:0007829|PDB:4GBU"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:4GBU"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:1K02"
FT TURN 300..303
FT /evidence="ECO:0007829|PDB:4GBU"
FT HELIX 312..316
FT /evidence="ECO:0007829|PDB:4GBU"
FT STRAND 321..326
FT /evidence="ECO:0007829|PDB:4GBU"
FT HELIX 331..337
FT /evidence="ECO:0007829|PDB:4GBU"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:4GBU"
FT HELIX 349..353
FT /evidence="ECO:0007829|PDB:4GBU"
FT HELIX 357..363
FT /evidence="ECO:0007829|PDB:4GBU"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:4GBU"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:4GBU"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:4GBU"
FT HELIX 389..394
FT /evidence="ECO:0007829|PDB:4GBU"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:4GBU"
SQ SEQUENCE 400 AA; 45015 MW; 0F3CA987E3EE1310 CRC64;
MSFVKDFKPQ ALGDTNLFKP IKIGNNELLH RAVIPPLTRM RALHPGNIPN RDWAVEYYTQ
RAQRPGTMII TEGAFISPQA GGYDNAPGVW SEEQMVEWTK IFNAIHEKKS FVWVQLWVLG
WAAFPDNLAR DGLRYDSASD NVFMDAEQEA KAKKANNPQH SLTKDEIKQY IKEYVQAAKN
SIAAGADGVE IHSANGYLLN QFLDPHSNTR TDEYGGSIEN RARFTLEVVD ALVEAIGHEK
VGLRLSPYGV FNSMSGGAET GIVAQYAYVA GELEKRAKAG KRLAFVHLVE PRVTNPFLTE
GEGEYEGGSN DFVYSIWKGP VIRAGNFALH PEVVREEVKD KRTLIGYGRF FISNPDLVDR
LEKGLPLNKY DRDTFYQMSA HGYIDYPTYE EALKLGWDKK
