[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-47. STRAIN=Brewer's bottom; PubMed=1939123 [NCBI, ExPASy, EBI, Israel, Japan] Saito K., Thiele D.J., Davio M., Lockridge O., Massey V.; "The cloning and expression of a gene encoding Old Yellow Enzyme from Saccharomyces carlsbergensis."; J. Biol. Chem. 266:20720-20724(1991).
[2]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH FMN AND SUBSTRATE. DOI=10.1016/S0969-2126(94)00111-1; PubMed=7881908 [NCBI, ExPASy, EBI, Israel, Japan] Fox K.M., Karplus P.A.; "Old yellow enzyme at 2-A resolution: overall structure, ligand binding, and comparison with related flavoproteins."; Structure 2:1089-1105(1994).
[3]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-399 IN COMPLEX WITH FMN, AND MUTAGENESIS OF HIS-192. DOI=10.1074/jbc.273.49.32753; PubMed=9830019 [NCBI, ExPASy, EBI, Israel, Japan] Brown B.J., Deng Z., Karplus P.A., Massey V.; "On the active site of Old Yellow Enzyme. Role of histidine 191 and asparagine 194."; J. Biol. Chem. 273:32753-32762(1998).
[4]	X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-400 OF MUTANT ASN-115 IN COMPLEX WITH FMN AND SUBSTRATE. DOI=10.1074/jbc.M108453200; PubMed=11668181 [NCBI, ExPASy, EBI, Israel, Japan] Brown B.J., Hyun J.-W., Duvvuri S., Karplus P.A., Massey V.; "The role of glutamine 114 in Old Yellow Enzyme."; J. Biol. Chem. 277:2138-2145(2002).

Comments

FUNCTION: Oxidizes beta-NADH, beta-NADPH, and alpha-NADPH.
CATALYTIC ACTIVITY: NADPH + acceptor = NADP⁺ + reduced acceptor.
COFACTOR: FMN.
SUBUNIT: Homodimer or heterodimer.
SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X53597; CAA37666.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A39495; A39495.

3D structure databases

PDB

1BWK; X-ray; 2.30 A; A=1-399.	[ExPASy / RCSB / EBI]
1BWL; X-ray; 2.70 A; A=1-399.	[ExPASy / RCSB / EBI]
1K02; X-ray; 2.70 A; A=1-400.	[ExPASy / RCSB / EBI]
1K03; X-ray; 2.70 A; A=1-400.	[ExPASy / RCSB / EBI]
1OYA; X-ray; 2.00 A; A=1-400.	[ExPASy / RCSB / EBI]
1OYB; X-ray; 2.00 A; A=1-400.	[ExPASy / RCSB / EBI]
1OYC; X-ray; 2.00 A; A=1-400.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1BWK; -.
1BWL; -.
1K02; -.
1K03; -.
1OYA; -.
1OYB; -.
1OYC; -.

ModBase

Q02899.

Ontologies

GO:0003959;	Molecular function: NADPH dehydrogenase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR013785; Aldolase_TIM.
IPR001155; OxRdtase_FMN_N.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.

Pfam

PF00724; Oxidored_FMN; 1.
Pfam graphical view of domain structure.

Other

Q02899; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; Flavoprotein; FMN; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 400`	`399`	`NADPH dehydrogenase 1.`	`PRO_0000194473`
`ACT_SITE`	`197 197`		`Proton donor (By similarity).`
`BINDING`	`38 38`		`FMN.`
`BINDING`	`192 192`		`FMN.`
`BINDING`	`192 192`		`Substrate.`
`BINDING`	`195 195`		`Substrate.`
`BINDING`	`244 244`		`FMN.`
`BINDING`	`349 349`		`FMN.`
`BINDING`	`376 376`		`Substrate.`
`MUTAGEN`	`115 115`		`Q->N: Strong reduction of substrate binding.`
`MUTAGEN`	`192 192`		`H->N: Strong reduction of substrate binding. Reduced oxidation of NADPH.`
`HELIX`	`16 18`	`3`
`STRAND`	`21 23`	`3`
`STRAND`	`26 34`	`9`
`TURN`	`44 47`	`4`
`TURN`	`51 53`	`3`
`HELIX`	`54 61`	`8`
`STRAND`	`68 77`	`10`
`HELIX`	`78 80`	`3`
`STRAND`	`88 91`	`4`
`HELIX`	`92 107`	`16`
`STRAND`	`111 117`	`7`
`HELIX`	`120 122`	`3`
`HELIX`	`125 130`	`6`
`STRAND`	`135 138`	`4`
`HELIX`	`146 154`	`9`
`STRAND`	`159 161`	`3`
`HELIX`	`164 183`	`20`
`STRAND`	`187 192`	`6`
`HELIX`	`198 203`	`6`
`TURN`	`205 207`	`3`
`STRAND`	`215 217`	`3`
`HELIX`	`218 236`	`19`
`HELIX`	`238 240`	`3`
`STRAND`	`241 245`	`5`
`TURN`	`251 253`	`3`
`HELIX`	`256 258`	`3`
`HELIX`	`262 278`	`17`
`STRAND`	`284 289`	`6`
`HELIX`	`312 316`	`5`
`STRAND`	`321 326`	`6`
`HELIX`	`331 337`	`7`
`STRAND`	`343 346`	`4`
`HELIX`	`349 353`	`5`
`HELIX`	`357 363`	`7`
`HELIX`	`372 374`	`3`
`STRAND`	`378 380`	`3`
`TURN`	`381 383`	`3`
`HELIX`	`389 394`	`6`

Sequence information

Length: 400 AA [This is the length of the unprocessed precursor]

Molecular weight: 45015 Da [This is the MW of the unprocessed precursor]

CRC64: 0F3CA987E3EE1310 [This is a checksum on the sequence]

        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

Q02899 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools