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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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei38 – 381FMN3 Publications
Binding sitei192 – 1921FMN3 Publications
Binding sitei192 – 1921Substrate2 Publications
Binding sitei195 – 1951Substrate2 Publications
Active sitei197 – 1971Proton donorBy similarity
Binding sitei244 – 2441FMN3 Publications
Binding sitei349 – 3491FMN3 Publications
Binding sitei376 – 3761Substrate2 Publications

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 1PRO_0000194473Add
BLAST

Interactioni

Subunit structurei

Homodimer or heterodimer.3 Publications

Structurei

Secondary structure

1
400
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 183Combined sources
Beta strandi21 – 233Combined sources
Beta strandi26 – 349Combined sources
Turni44 – 474Combined sources
Turni51 – 533Combined sources
Helixi54 – 618Combined sources
Beta strandi68 – 703Combined sources
Beta strandi74 – 774Combined sources
Helixi78 – 803Combined sources
Beta strandi88 – 914Combined sources
Helixi92 – 10716Combined sources
Beta strandi111 – 1177Combined sources
Helixi120 – 1223Combined sources
Helixi125 – 1306Combined sources
Beta strandi136 – 1383Combined sources
Beta strandi140 – 1423Combined sources
Helixi146 – 1549Combined sources
Beta strandi159 – 1613Combined sources
Helixi164 – 18320Combined sources
Beta strandi187 – 1926Combined sources
Helixi198 – 2036Combined sources
Turni205 – 2073Combined sources
Beta strandi215 – 2173Combined sources
Helixi218 – 2214Combined sources
Helixi223 – 23614Combined sources
Helixi238 – 2403Combined sources
Beta strandi241 – 2455Combined sources
Turni251 – 2533Combined sources
Helixi256 – 2583Combined sources
Helixi262 – 27817Combined sources
Beta strandi284 – 2896Combined sources
Beta strandi296 – 2983Combined sources
Turni300 – 3034Combined sources
Helixi312 – 3165Combined sources
Beta strandi321 – 3266Combined sources
Helixi331 – 3377Combined sources
Beta strandi343 – 3464Combined sources
Helixi349 – 3535Combined sources
Helixi357 – 3637Combined sources
Helixi372 – 3743Combined sources
Beta strandi378 – 3803Combined sources
Turni381 – 3833Combined sources
Helixi389 – 3946Combined sources
Helixi397 – 3993Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

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

        10         20         30         40         50
MSFVKDFKPQ ALGDTNLFKP IKIGNNELLH RAVIPPLTRM RALHPGNIPN
60 70 80 90 100
RDWAVEYYTQ RAQRPGTMII TEGAFISPQA GGYDNAPGVW SEEQMVEWTK
110 120 130 140 150
IFNAIHEKKS FVWVQLWVLG WAAFPDNLAR DGLRYDSASD NVFMDAEQEA
160 170 180 190 200
KAKKANNPQH SLTKDEIKQY IKEYVQAAKN SIAAGADGVE IHSANGYLLN
210 220 230 240 250
QFLDPHSNTR TDEYGGSIEN RARFTLEVVD ALVEAIGHEK VGLRLSPYGV
260 270 280 290 300
FNSMSGGAET GIVAQYAYVA GELEKRAKAG KRLAFVHLVE PRVTNPFLTE
310 320 330 340 350
GEGEYEGGSN DFVYSIWKGP VIRAGNFALH PEVVREEVKD KRTLIGYGRF
360 370 380 390 400
FISNPDLVDR LEKGLPLNKY DRDTFYQMSA HGYIDYPTYE EALKLGWDKK
Length:400
Mass (Da):45,015
Last modified:January 23, 2007 - v3
Checksum:i0F3CA987E3EE1310
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53597 Genomic DNA. Translation: CAA37666.1.
PIRiA39495.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53597 Genomic DNA. Translation: CAA37666.1 .
PIRi A39495.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 88 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