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

CP000668; ABP41876.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001164849.1; -.

3D structure databases

ModBase

A4TRG4.

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

A4TRG4.

Genome annotation databases

GeneID

5062064; -.

GenomeReviews

CP000668_GR; YPDSF_3526.

KEGG

ypp:YPDSF_3526; -.

CMR

A4TRG4; YPDSF_3526.

Other

ProtoNet

A4TRG4.

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`	`1 466`	`466`	`Soluble pyridine nucleotide transhydrogenase.`	`PRO_1000012568`
`NP_BIND`	`36 45`	`10`	`FAD (By similarity).`

Sequence information

Length: 466 AA [This is the length of the unprocessed precursor]

Molecular weight: 51382 Da [This is the MW of the unprocessed precursor]

CRC64: D6CD965D6CF3E2CE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQQHFHFDAI VIGSGPGGEG AAMGLVKQGA RVAVIERYNN VGGGCTHWGT IPSKALRHAV 

        70         80         90        100        110        120 
SRIIEFNQNP LYSDNARTIK SSFADILNHA DRVINQQTRM RQGFYDRNHC HMFSGDASFI 

       130        140        150        160        170        180 
DANTVNVRYA DGTSDTLQAD NIVIATGSRP YRPVNVDFNH ERIYDSDTIL QLSHEPQHVI 

       190        200        210        220        230        240 
IYGAGVIGCE YASIFRGLSV KVDLINTRDR LLAFLDQEMS DALSYHFWNN GVVIRHNEEF 

       250        260        270        280        290        300 
EQIEGTTDGV IVHLKSGKKV KADCLLYANG RTGNTSGLGL ENIGLEADSR GLLKVNSMYQ 

       310        320        330        340        350        360 
TALSHVYAVG DVIGYPSLAS AAYDQGRIAA QAMIKGEANV HLIEDIPTGI YTIPEISSVG 

       370        380        390        400        410        420 
KTEQELTAMK VPYEVGRAQF KHLARAQIVG MDTGSLKILF HRETKQILGI HCFGERAAEI 

       430        440        450        460 
IHIGQAIMEQ KGEGNTLEYF VNTTFNYPTM AEAYRVAALN GLNRLF

A4TRG4 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