Reviewed, UniProtKB/Swiss-Prot Q02899 (OYE1_SACPS)

Names and origin

Protein names

Recommended name:
    NADPH dehydrogenase 1
    EC=1.6.99.1
Alternative name(s):
    Old yellow enzyme 1

Gene names

Name:

OYE1

Organism

Saccharomyces pastorianus (Lager yeast) (Saccharomyces carlsbergensis)

Taxonomic identifier

27292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	400 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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
Ligand	FMN Flavoprotein NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FMN binding Inferred from electronic annotation. Source: InterPro NADPH dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 400

399

NADPH dehydrogenase 1

PRO_0000194473

Sites

Active site

197

1

Proton donor By similarity

Binding site

38

1

FMN

Binding site

192

1

FMN

Binding site

192

1

Substrate

Binding site

195

1

Substrate

Binding site

244

1

FMN

Binding site

349

1

FMN

Binding site

376

1

Substrate

Experimental info

Mutagenesis

115

1

Q → N: Strong reduction of substrate binding

Mutagenesis

192

1

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

Secondary structure

1

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400

Helix Strand Turn

Details...

Helix

16 – 18

3

Beta strand

21 – 23

3

Beta strand

26 – 34

9

Turn

44 – 47

4

Turn

51 – 53

3

Helix

54 – 61

8

Beta strand

68 – 77

10

Helix

78 – 80

3

Beta strand

88 – 91

4

Helix

92 – 107

16

Beta strand

111 – 117

7

Helix

120 – 122

3

Helix

125 – 130

6

Beta strand

135 – 138

4

Helix

146 – 154

9

Beta strand

159 – 161

3

Helix

164 – 183

20

Beta strand

187 – 192

6

Helix

198 – 203

6

Turn

205 – 207

3

Beta strand

215 – 217

3

Helix

218 – 221

4

Helix

223 – 236

14

Helix

238 – 240

3

Beta strand

241 – 245

5

Turn

251 – 253

3

Helix

256 – 258

3

Helix

262 – 278

17

Beta strand

284 – 289

6

Helix

312 – 316

5

Beta strand

321 – 326

6

Helix

331 – 337

7

Beta strand

343 – 346

4

Helix

349 – 353

5

Helix

357 – 363

7

Helix

372 – 374

3

Beta strand

378 – 380

3

Turn

381 – 383

3

Helix

389 – 394

6

Sequences

	Sequence		Length	Mass (Da)
	Q02899-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 0F3CA987E3EE1310	FASTA	400	45,015
	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

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

EMBLGenBankDDBJ

X53597 Genomic DNA. Translation: CAA37666.1.

PIR

A39495.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BWK	X-ray	2.30	A	1-399	[»]
1BWL	X-ray	2.70	A	1-399	[»]
1K02	X-ray	2.70	A	1-400	[»]
1K03	X-ray	2.70	A	1-400	[»]
1OYA	X-ray	2.00	A	1-400	[»]
1OYB	X-ray	2.00	A	1-400	[»]
1OYC	X-ray	2.00	A	1-400	[»]

ModBase

Search...

Family and domain databases

InterPro

IPR013785. Aldolase_TIM.
IPR001155. OxRdtase_FMN_N.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

Pfam

PF00724. Oxidored_FMN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

Q02899.

Entry information

Entry name

OYE1_SACPS

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)