[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228; DOI=10.1038/35023079; PubMed=10984043 [NCBI, ExPASy, EBI, Israel, Japan] Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."; Nature 406:959-964(2000).
[2]	CHARACTERIZATION. DOI=10.1016/0003-9861(76)90149-1; PubMed=823872 [NCBI, ExPASy, EBI, Israel, Japan] Wermuth B., Kaplan N.O.; "Pyridine nucleotide transhydrogenase from Pseudomonas aeruginosa: purification by affinity chromatography and physicochemical properties."; Arch. Biochem. Biophys. 176:136-143(1976).
[3]	CHARACTERIZATION. DOI=10.1016/0006-291X(77)90995-0; PubMed=20086 [NCBI, ExPASy, EBI, Israel, Japan] Widmer F., Kaplan N.O.; "Pseudomonas aeruginosa transhydrogenase: affinity of substrates for the regulatory site and possible hysteretic behavior."; Biochem. Biophys. Res. Commun. 76:1287-1292(1977).

Comments

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.
ENZYME REGULATION: Strongly activated by NADPH and 2'-AMP and inhibited by NADP(+). Ca(2+) increases the activation and decreases the inhibition effect.
SUBUNIT: Homooligomer; probably composed of four stacked rings of 7 or 8 monomers. Forms filamentous structures.
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

AE004091; AAG06379.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

H83271; H83271.

RefSeq

NP_251681.1; -.

3D structure databases

HSSP

P11959; 1EBD. [HSSP ENTRY / PDB]

ModBase

P57112.

Enzyme and pathway databases

BioCyc

PAER208964:PA2991-MON; -.

Organism-specific databases

PseudoCAP

PA2991; -.

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

P57112.

Genome annotation databases

GeneID

878679; -.

GenomeReviews

AE004091_GR; PA2991.

KEGG

pae:PA2991; -.

Phylogenomic databases

HOGENOM

P57112; -.

Genome annotation databases

CMR

P57112; PA2991.

Other

ProtoNet

P57112.

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`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 464`	`463`	`Soluble pyridine nucleotide transhydrogenase.`	`PRO_0000068068`
`NP_BIND`	`35 44`	`10`	`FAD (By similarity).`

Sequence information

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

Molecular weight: 51161 Da [This is the MW of the unprocessed precursor]

CRC64: 886CEAB5479997A9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVYNYDVVI LGTGPAGEGA AMNASKYGRK LAVVDSRRVV GGNCTHLGTI PSKALRHSVK 

        70         80         90        100        110        120 
QIIEFNTNPM FRQIGEPRWF SFPDVLKSAD RVISKQVASR TGYYARNRID MFTGTASFVD 

       130        140        150        160        170        180 
ERTVEVVTPS GAVERLVADQ FVIATGSRPY RPSDINFNHP RVYDSDTILS LSHTPRRLII 

       190        200        210        220        230        240 
YGAGVIGCEY ASIFSGLGVL VDLIDTRDQL LSFLDDEISD ALSYHLRNNN VLIRHNEEYE 

       250        260        270        280        290        300 
RVEGLDNGVI LHLKSGKKIK ADALLWCNGR TGNTDKLGLE NVGIKVNSRG QIEVDENYRT 

       310        320        330        340        350        360 
SVSNIFAAGD VIGWPSLASA AYDQGRSAAG NIVESDSWRF VNDVPTGIYT IPEISSIGKN 

       370        380        390        400        410        420 
ESELTAAKIP YEVGKAFFKG MARAQISNEP VGMLKILFHR ETLEILGVHC FGDQASEIVH 

       430        440        450        460 
IGQAIMNQPG ELNTLKYFVN TTFNYPTMAE AYRVAAFDGL NRLF

P57112 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