[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 478 / NRS 16 / DSM 2289 / VKM B-1617; DOI=10.1111/j.1574-6968.2000.tb09323.x; PubMed=11004404 [NCBI, ExPASy, EBI, Israel, Japan] Boonstra B., Bjorklund L., French C.E., Wainwright I., Bruce N.C.; "Cloning of the sth gene from Azotobacter vinelandii and construction of chimeric soluble pyridine nucleotide transhydrogenases."; FEMS Microbiol. Lett. 191:87-93(2000).
[2]	CHARACTERIZATION. STRAIN=ATCC 478 / NRS 16 / DSM 2289 / VKM B-1617; PubMed=7460901 [NCBI, ExPASy, EBI, Israel, Japan] Voordouw G., van der Vies S.M., Eweg J.K., Veeger C., van Breemen J.F.L., van Bruggen E.F.J.; "Pyridine nucleotide transhydrogenase from Azotobacter vinelandii. Improved purification, physical properties and subunit arrangement in purified polymers."; Eur. J. Biochem. 111:347-355(1980).
[3]	SUBUNIT. STRAIN=ATCC 478 / NRS 16 / DSM 2289 / VKM B-1617; PubMed=39756 [NCBI, ExPASy, EBI, Israel, Japan] Voordouw G., Veeger C., van Breemen J.F.L., van Bruggen E.F.J.; "Structure of pyridine nucleotide transhydrogenase from Azotobacter vinelandii."; Eur. J. Biochem. 98:447-454(1979).

Comments

FUNCTION: Conversion of NADPH, generated by peripheral catabolic pathways, to NADH, which can enter the respiratory chain for energy generation.
CATALYTIC ACTIVITY: NADPH + NAD⁺ = NADP⁺ + NADH.
COFACTOR: Binds 1 FAD per subunit.
SUBUNIT: Homooctamer. Forms a polymeric filamentous structure in purified form.
SUBCELLULAR LOCATION: Cytoplasm.
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

AF159108; AAD40691.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P14218; 1LPF. [HSSP ENTRY / PDB]

ModBase

Q9XBQ9.

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

IPR000759; Adrndx_reductase.
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

PR00419; ADXRDTASE.
PR00368; FADPNR.
PR00945; HGRDTASE.
PR00411; PNDRDTASEI.

ProDom

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

Other

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

Keywords

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_0000068060`
`NP_BIND`	`35 44`	`10`	`FAD (By similarity).`

Sequence information

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

Molecular weight: 51331 Da [This is the MW of the unprocessed precursor]

CRC64: B67F2A3365CE0781 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVYNYDVVV IGTGPAGEGA AMNAVKAGRK VAVVDDRPQV GGNCTHLGTI PSKALRHSVR 

        70         80         90        100        110        120 
QIMQYNNNPL FRQIGEPRWF SFADVLKSAE QVIAKQVSSR TGYYARNRID TFFGTASFCD 

       130        140        150        160        170        180 
EHTIEVVHLN GMVETLVAKQ FVIATGSRPY RPADVDFTHP RIYDSDTILS LGHTPRRLII 

       190        200        210        220        230        240 
YGAGVIGCEY ASIFSGLGVL VDLIDNRDQL LSFLDDEISD SLSYHLRNNN VLIRHNEEYE 

       250        260        270        280        290        300 
RVEGLDNGVI LHLKSGKKIK ADAFLWSNGR TGNTDKLGLE NIGLKANGRG QIQVDEHYRT 

       310        320        330        340        350        360 
EVSNIYAAGD VIGWPSLASA AYDQGRSAAG SITENDSWRF VDDVPTGIYT IPEISSVGKT 

       370        380        390        400        410        420 
ERELTQAKVP YEVGKAFFKG MARAQIAVEK AGMLKILFHR ETLEILGVHC FGYQASEIVH 

       430        440        450        460 
IGQAIMNQKG EANTLKYFIN TTFNYPTMAE AYRVAAYDGL NRLF

Q9XBQ9 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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