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

CP000627; ABQ21088.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001218270.1; -.

3D structure databases

ModBase

A5F4K5.

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

A5F4K5.

Genome annotation databases

GeneID

5135852; -.

GenomeReviews

CP000627_GR; VC0395_A2370.

KEGG

vco:VC0395_A2370; -.

CMR

A5F4K5; VC0395_A2370.

Other

ProtoNet

A5F4K5.

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_1000071844`
`NP_BIND`	`36 45`	`10`	`FAD (By similarity).`

Sequence information

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

Molecular weight: 50942 Da [This is the MW of the unprocessed precursor]

CRC64: 60D05DB3FD595BE1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGQKNHFDVI VIGSGPGGEG AAMGLTKGGK NVAIIEKESS VGGGCTHWGT IPSKALRHAV 

        70         80         90        100        110        120 
SRIIEFNSNP LFCKNNSSIH ATFSTILSHA KSVIDKQTRL RQGFYDRNQC TLIFGAAHFI 

       130        140        150        160        170        180 
DAHTVAVKKA DGSIDTYSAD KFVIATGSRP YHPKDVDFGH PRIYDSDSIL NLEHDPRHII 

       190        200        210        220        230        240 
IYGAGVIGCE YASIFRGLDV KTDLINTRDR LLSFLDNEVS DALSYHFWNS GVVIRNDETY 

       250        260        270        280        290        300 
DKVEGTSDGV IVHLKSGKKM RADCLLYANG RTGNTDKLNL ESVGLQADSR GQLVVNANYQ 

       310        320        330        340        350        360 
TQVEHIYAVG DVIGYPSLAS AAYDQGRFVA QAIIHGQAAH LLTEDIPTGI YTIPEISSVG 

       370        380        390        400        410        420 
RTEQELTAAK VPYEVGRASF KHLARAQIAG KDIGSLKILF HRETKEILGI HCFGERAAEI 

       430        440        450        460 
IHIGQAIMEQ KGEANTIEYF VNTTFNYPTM AEAFRVAALN GLNRLF

A5F4K5 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