FUNCTION: Conversion of NADPH, generated by peripheral catabolic pathways, to NADH, which can enter the respiratory chain for energy generation (By similarity).
CATALYTIC ACTIVITY: NADPH + NAD⁺ = NADP⁺ + NADH.
COFACTOR: Binds 1 FAD per subunit (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase 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

CP000926; ABY97595.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001667931.1; -.

3D structure databases

ModBase

B0KH90.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0003957;	Molecular function: NAD(P)+ transhydrogenase (B-specific) activity (inferred from electronic annotation from HAMAP).
GO:0006739;	Biological process: NADP metabolic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00247; -; 1.
PBIL [Tree]

InterPro

IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000815; Hg_reductase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.390.30; Pyr_redox_dim; 1.

Pfam

PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
PF02852; Pyr_redox_dim; 1.
Pfam graphical view of domain structure.

PRINTS

PR00368; FADPNR.
PR00945; HGRDTASE.
PR00411; PNDRDTASEI.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

BLOCKS

B0KH90.

Genome annotation databases

GeneID

5869472; -.

GenomeReviews

CP000926_GR; PputGB1_1692.

KEGG

ppg:PputGB1_1692; -.

CMR

B0KH90; PputGB1_1692.

Other

ProtoNet

B0KH90.

UniRef

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

Keywords

Complete proteome; Cytoplasm; FAD; Flavoprotein; NAD; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 464`	`464`	`Soluble pyridine nucleotide transhydrogenase.`	`PRO_1000078412`
`NP_BIND`	`35 44`	`10`	`FAD (By similarity).`

Sequence information

Length: 464 AA [This is the length of the unprocessed precursor]

Molecular weight: 50949 Da [This is the MW of the unprocessed precursor]

CRC64: 32DA105F9B0C39AD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVYNYDVVV LGSGPAGEGA AMNAAKAGRK VAMVDDRRQV GGNCTHLGTI PSKALRHSVR 

        70         80         90        100        110        120 
QIMQFNTNPM FRAIGEPRWF SFPDVLKSAE KVISKQVASR TGYYARNRVD VFFGTGSFAD 

       130        140        150        160        170        180 
EQTVEVVCPN GVVEKLNAKH IIIATGSRPY RPADIDFHHP RVYDSDTILS LSHTPRKLIV 

       190        200        210        220        230        240 
YGAGVIGCEY ASIFSGLGVL VELVDNRGQL LSFLDSEISQ ALSYHFSNNN ITVRHNEEYE 

       250        260        270        280        290        300 
RVEGLDNGVI LHLKSGKKIK ADALLWCNGR TGNTDKLGLE NIGIKVNSRG QIEVDEAYRT 

       310        320        330        340        350        360 
TVPNIYGAGD VIGWPSLASA AHDQGRSAAG SIVDNGSWRF VNDVPTGIYT IPEISSIGKN 

       370        380        390        400        410        420 
EQELTQAKVP YEVGKAFFKG MARAQIAGEP QGMLKILFHR ETLEILGVHC FGYQASEIVH 

       430        440        450        460 
IGQAIMNQPG EHNNLKYFVN TTFNYPTMAE AYRVAAYDGL NRLF

B0KH90 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