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Q02899

- OYE1_SACPS

UniProt

Q02899 - OYE1_SACPS

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Protein
NADPH dehydrogenase 1
Gene
OYE1
Organism
Saccharomyces pastorianus (Lager yeast) (Saccharomyces cerevisiae x Saccharomyces eubayanus)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Oxidizes beta-NADH, beta-NADPH, and alpha-NADPH.

Catalytic activityi

NADPH + acceptor = NADP+ + reduced acceptor.

Cofactori

FMN.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei38 – 381FMN
Binding sitei192 – 1921FMN
Binding sitei192 – 1921Substrate
Binding sitei195 – 1951Substrate
Active sitei197 – 1971Proton donor By similarity
Binding sitei244 – 2441FMN
Binding sitei349 – 3491FMN
Binding sitei376 – 3761Substrate

GO - Molecular functioni

  1. FMN binding Source: InterPro
  2. NADPH dehydrogenase activity Source: UniProtKB-EC
  3. pentaerythritol trinitrate reductase activity Source: UniProtKB-EC
  4. trichloro-p-hydroquinone reductive dehalogenase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
NADPH dehydrogenase 1 (EC:1.6.99.1)
Alternative name(s):
Old yellow enzyme 1
Gene namesi
Name:OYE1
OrganismiSaccharomyces pastorianus (Lager yeast) (Saccharomyces cerevisiae x Saccharomyces eubayanus)
Taxonomic identifieri27292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi115 – 1151Q → N: Strong reduction of substrate binding.
Mutagenesisi192 – 1921H → N: Strong reduction of substrate binding. Reduced oxidation of NADPH. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 400399NADPH dehydrogenase 1
PRO_0000194473Add
BLAST

Interactioni

Subunit structurei

Homodimer or heterodimer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 183
Beta strandi21 – 233
Beta strandi26 – 349
Turni44 – 474
Turni51 – 533
Helixi54 – 618
Beta strandi68 – 703
Beta strandi74 – 774
Helixi78 – 803
Beta strandi88 – 914
Helixi92 – 10716
Beta strandi111 – 1177
Helixi120 – 1223
Helixi125 – 1306
Beta strandi136 – 1383
Beta strandi140 – 1423
Helixi146 – 1549
Beta strandi159 – 1613
Helixi164 – 18320
Beta strandi187 – 1926
Helixi198 – 2036
Turni205 – 2073
Beta strandi215 – 2173
Helixi218 – 2214
Helixi223 – 23614
Helixi238 – 2403
Beta strandi241 – 2455
Turni251 – 2533
Helixi256 – 2583
Helixi262 – 27817
Beta strandi284 – 2896
Beta strandi296 – 2983
Turni300 – 3034
Helixi312 – 3165
Beta strandi321 – 3266
Helixi331 – 3377
Beta strandi343 – 3464
Helixi349 – 3535
Helixi357 – 3637
Helixi372 – 3743
Beta strandi378 – 3803
Turni381 – 3833
Helixi389 – 3946
Helixi397 – 3993

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BWKX-ray2.30A2-399[»]
1BWLX-ray2.70A2-399[»]
1K02X-ray2.70A2-400[»]
1K03X-ray2.70A2-400[»]
1OYAX-ray2.00A1-400[»]
1OYBX-ray2.00A1-400[»]
1OYCX-ray2.00A1-400[»]
3RNDX-ray1.40A2-400[»]
3TX9X-ray2.00A1-400[»]
3TXZX-ray1.70A1-400[»]
4GBUX-ray1.18A1-400[»]
4GE8X-ray1.50A1-400[»]
4GWEX-ray1.45A1-400[»]
4GXMX-ray1.36A1-400[»]
4H4IX-ray1.25A1-400[»]
4H6KX-ray1.55A2-400[»]
4K7VX-ray1.52A1-400[»]
4K7YX-ray1.20A1-400[»]
4K8EX-ray1.27A1-400[»]
4K8HX-ray1.55A1-400[»]
ProteinModelPortaliQ02899.
SMRiQ02899. Positions 2-400.

Miscellaneous databases

EvolutionaryTraceiQ02899.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR001155. OxRdtase_FMN_N.
[Graphical view]
PfamiPF00724. Oxidored_FMN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q02899-1 [UniParc]FASTAAdd to Basket

« Hide

MSFVKDFKPQ ALGDTNLFKP IKIGNNELLH RAVIPPLTRM RALHPGNIPN    50
RDWAVEYYTQ RAQRPGTMII TEGAFISPQA GGYDNAPGVW SEEQMVEWTK 100
IFNAIHEKKS FVWVQLWVLG WAAFPDNLAR DGLRYDSASD NVFMDAEQEA 150
KAKKANNPQH SLTKDEIKQY IKEYVQAAKN SIAAGADGVE IHSANGYLLN 200
QFLDPHSNTR TDEYGGSIEN RARFTLEVVD ALVEAIGHEK VGLRLSPYGV 250
FNSMSGGAET GIVAQYAYVA GELEKRAKAG KRLAFVHLVE PRVTNPFLTE 300
GEGEYEGGSN DFVYSIWKGP VIRAGNFALH PEVVREEVKD KRTLIGYGRF 350
FISNPDLVDR LEKGLPLNKY DRDTFYQMSA HGYIDYPTYE EALKLGWDKK 400
Length:400
Mass (Da):45,015
Last modified:January 23, 2007 - v3
Checksum:i0F3CA987E3EE1310
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X53597 Genomic DNA. Translation: CAA37666.1.
PIRiA39495.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X53597 Genomic DNA. Translation: CAA37666.1 .
PIRi A39495.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BWK X-ray 2.30 A 2-399 [» ]
1BWL X-ray 2.70 A 2-399 [» ]
1K02 X-ray 2.70 A 2-400 [» ]
1K03 X-ray 2.70 A 2-400 [» ]
1OYA X-ray 2.00 A 1-400 [» ]
1OYB X-ray 2.00 A 1-400 [» ]
1OYC X-ray 2.00 A 1-400 [» ]
3RND X-ray 1.40 A 2-400 [» ]
3TX9 X-ray 2.00 A 1-400 [» ]
3TXZ X-ray 1.70 A 1-400 [» ]
4GBU X-ray 1.18 A 1-400 [» ]
4GE8 X-ray 1.50 A 1-400 [» ]
4GWE X-ray 1.45 A 1-400 [» ]
4GXM X-ray 1.36 A 1-400 [» ]
4H4I X-ray 1.25 A 1-400 [» ]
4H6K X-ray 1.55 A 2-400 [» ]
4K7V X-ray 1.52 A 1-400 [» ]
4K7Y X-ray 1.20 A 1-400 [» ]
4K8E X-ray 1.27 A 1-400 [» ]
4K8H X-ray 1.55 A 1-400 [» ]
ProteinModelPortali Q02899.
SMRi Q02899. Positions 2-400.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q02899.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR001155. OxRdtase_FMN_N.
[Graphical view ]
Pfami PF00724. Oxidored_FMN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The cloning and expression of a gene encoding Old Yellow Enzyme from Saccharomyces carlsbergensis."
    Saito K., Thiele D.J., Davio M., Lockridge O., Massey V.
    J. Biol. Chem. 266:20720-20724(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-47.
    Strain: Brewer's bottom.
  2. "Old yellow enzyme at 2-A resolution: overall structure, ligand binding, and comparison with related flavoproteins."
    Fox K.M., Karplus P.A.
    Structure 2:1089-1105(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH FMN AND SUBSTRATE.
  3. "On the active site of Old Yellow Enzyme. Role of histidine 191 and asparagine 194."
    Brown B.J., Deng Z., Karplus P.A., Massey V.
    J. Biol. Chem. 273:32753-32762(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-399 IN COMPLEX WITH FMN, MUTAGENESIS OF HIS-192.
  4. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-400 OF MUTANT ASN-115 IN COMPLEX WITH FMN AND SUBSTRATE.

Entry informationi

Entry nameiOYE1_SACPS
AccessioniPrimary (citable) accession number: Q02899
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 86 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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