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Q02899 (OYE1_SACPS) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
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. Ref.3

Secondary structure

1 ................................................................................... 400
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q02899 [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] [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]"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] [Europe PMC] [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

EMBL
GenBank
DDBJ		X53597 Genomic DNA. Translation: CAA37666.1.
PIRA39495.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ02899.
SMRQ02899. Positions 2-400.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR001155. OxRdtase_FMN_N.
[Graphical view]
PfamPF00724. Oxidored_FMN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ02899.

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: April 3, 2013
This is version 83 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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