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

CP000826; ABV43867.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001480995.1; -.

3D structure databases

ModBase

A8GL77.

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

A8GL77.

Genome annotation databases

GeneID

5604663; -.

GenomeReviews

CP000826_GR; Spro_4774.

KEGG

spe:Spro_4774; -.

CMR

A8GL77; Spro_4774.

Other

ProtoNet

A8GL77.

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`	`1 465`	`465`	`Soluble pyridine nucleotide transhydrogenase.`	`PRO_1000059011`
`NP_BIND`	`36 45`	`10`	`FAD (By similarity).`

Sequence information

Length: 465 AA [This is the length of the unprocessed precursor]

Molecular weight: 51218 Da [This is the MW of the unprocessed precursor]

CRC64: 333239320BC80F3F [This is a checksum on the sequence]

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

        70         80         90        100        110        120 
SRIIEFNQNP LYNNSRTLSA TFPDILRHAD NVINQQTRMR QGFYERNQCK LFAGDARFID 

       130        140        150        160        170        180 
ANTVSVSYMD GTQDTIRADH IVIACGSRPY NPSSVDFNHP RIYNSDSILE LNHEPRHVII 

       190        200        210        220        230        240 
YGAGVIGCEY ASIFRGLNVK VDLINTRDRL LAFLDQEMSD SLSYHFWNNG VVIRHNEEFE 

       250        260        270        280        290        300 
KIEGTDDGVI VHLKSGKKVK ADCLLYANGR TGNTDSLGLE NVGLESDSRG LLKVNSMYQT 

       310        320        330        340        350        360 
ALSHIYAVGD VIGYPSLASA AYDQGRIAAQ AIASGEASGH LIEDIPTGIY TIPEISSVGK 

       370        380        390        400        410        420 
TEQELTAMKV PYEVGRAQFK HLARAQIAGM NVGSLKILFH RDTLQILGIH CFGERAAEII 

       430        440        450        460 
HIGQAIMEQK GEGNTIEYFV NTTFNYPTMA EAYRVAALNG LNRLF

A8GL77 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