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Reviewed, UniProtKB/Swiss-Prot Q02899 (OYE1_SACPS)

Last modified November 25, 2008. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    NADPH dehydrogenase 1
    EC=1.6.99.1
Alternative name(s):
    Old yellow enzyme 1
Gene names
Name: OYE1
OrganismSaccharomyces pastorianus (Lager yeast) (Saccharomyces carlsbergensis)
Taxonomic identifier27292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length400 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

Catalytic activity

NADPH + acceptor = NADP(+) + reduced acceptor.

Cofactor

FMN.

Subunit structure

Homodimer or heterodimer.

Sequence similarities

Belongs to the NADH:flavin oxidoreductase/NADH oxidase family.

Ontologies

Keywords

   LigandFMN
Flavoprotein
NADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Direct protein sequencing

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionFMN binding

Inferred from electronic annotation. Source: InterPro

NADPH dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 400399NADPH dehydrogenase 1
PRO_0000194473

Sites

Active site1971Proton donor By similarity
Binding site381FMN
Binding site1921FMN
Binding site1921Substrate
Binding site1951Substrate
Binding site2441FMN
Binding site3491FMN
Binding site3761Substrate

Experimental info

Mutagenesis1151Q → N: Strong reduction of substrate binding
Mutagenesis1921H → N: Strong reduction of substrate binding. Reduced oxidation of NADPH

Secondary structure

......................................................................... 400
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q02899-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 0F3CA987E3EE1310

FASTA40045,015
        10         20         30         40         50         60 
MSFVKDFKPQ ALGDTNLFKP IKIGNNELLH RAVIPPLTRM RALHPGNIPN RDWAVEYYTQ 

        70         80         90        100        110        120 
RAQRPGTMII TEGAFISPQA GGYDNAPGVW SEEQMVEWTK IFNAIHEKKS FVWVQLWVLG 

       130        140        150        160        170        180 
WAAFPDNLAR DGLRYDSASD NVFMDAEQEA KAKKANNPQH SLTKDEIKQY IKEYVQAAKN 

       190        200        210        220        230        240 
SIAAGADGVE IHSANGYLLN QFLDPHSNTR TDEYGGSIEN RARFTLEVVD ALVEAIGHEK 

       250        260        270        280        290        300 
VGLRLSPYGV FNSMSGGAET GIVAQYAYVA GELEKRAKAG KRLAFVHLVE PRVTNPFLTE 

       310        320        330        340        350        360 
GEGEYEGGSN DFVYSIWKGP VIRAGNFALH PEVVREEVKD KRTLIGYGRF FISNPDLVDR 

       370        380        390        400 
LEKGLPLNKY DRDTFYQMSA HGYIDYPTYE EALKLGWDKK 

« Hide

References

[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: 1939123] [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: 7881908] [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: 9830019] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-399 IN COMPLEX WITH FMN, MUTAGENESIS OF HIS-192.
[4]"The role of glutamine 114 in Old Yellow Enzyme."
Brown B.J., Hyun J.-W., Duvvuri S., Karplus P.A., Massey V.
J. Biol. Chem. 277:2138-2145(2002) [PubMed: 11668181] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-400 OF MUTANT ASN-115 IN COMPLEX WITH FMN AND SUBSTRATE.

Cross-references

Sequence databases

X53597 Genomic DNA. Translation: CAA37666.1.
PIRA39495.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1BWKX-ray2.30A1-399[»]
1BWLX-ray2.70A1-399[»]
1K02X-ray2.70A1-400[»]
1K03X-ray2.70A1-400[»]
1OYAX-ray2.00A1-400[»]
1OYBX-ray2.00A1-400[»]
1OYCX-ray2.00A1-400[»]
ModBaseSearch...

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR001155. OxRdtase_FMN_N.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PfamPF00724. Oxidored_FMN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

LinkHubQ02899.

Entry information

Entry nameOYE1_SACPS
AccessionPrimary (citable) accession number: Q02899
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: November 25, 2008
This is version 64 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents