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

CP000680; ABP84367.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001187099.1; -.

3D structure databases

ModBase

A4XSQ1.

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

A4XSQ1.

Genome annotation databases

GeneID

5109261; -.

GenomeReviews

CP000680_GR; Pmen_1603.

KEGG

pmy:Pmen_1603; -.

CMR

A4XSQ1; Pmen_1603.

Other

ProtoNet

A4XSQ1.

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_1000012564`
`NP_BIND`	`35 44`	`10`	`FAD (By similarity).`

Sequence information

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

Molecular weight: 51015 Da [This is the MW of the unprocessed precursor]

CRC64: 7F403879A82E3C7F [This is a checksum on the sequence]

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

        70         80         90        100        110        120 
QIMQFNTNPM FRQIGEPRWF SFPDVLKSAE KVIAKQVTSR TGYYARNRID TYFGTASFAD 

       130        140        150        160        170        180 
EQTVEVVCLN GVVEKLVAKQ IVIATGSRPY RPADVDFRHP RIYDSDTILS LGHTPRRLII 

       190        200        210        220        230        240 
YGAGVIGCEY ASIFSGLGVL VDLIDNRDQL LSFLDSEISD ALSYHLRNNN VLIRHNEEYE 

       250        260        270        280        290        300 
RIEGVENGVV LHLKSGKKIK ADALLWCNGR TGNTDQLGLE NIGIAVNSRG QIQVDEHYRT 

       310        320        330        340        350        360 
EVSNIYAAGD VIGWPSLASA AADQGRSAAG SIVENGSWRF VDDVPTGIYT IPEISSIGKT 

       370        380        390        400        410        420 
ERELTQAKVP YEVGKAFFKG MARAQISVEP VGMLKILFHR ETLEVLGVHC FGYQASEIVH 

       430        440        450        460 
IGQAIMNQKG EANSIKYFIN TTFNYPTMAE AYRVAAFDGL NRLF

A4XSQ1 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