EC 1.6.1.2
Nicotinamide nucleotide transhydrogenase subunit beta
Pyridine nucleotide transhydrogenase subunit beta
Proton-translocating transhydrogenase NADP(H)-binding component
dIII

Gene name

	Name:	pntB
	Synonyms:	nntB

From

Rhodospirillum rubrum

[TaxID: 1085]

Taxonomy

Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; Rhodospirillaceae; Rhodospirillum.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/BF00762784; PubMed=7844118 [NCBI, ExPASy, EBI, Israel, Japan] Yamaguchi M., Hatefi Y.; "Energy-transducing nicotinamide nucleotide transhydrogenase: nucleotide sequences of the genes and predicted amino acid sequences of the subunits of the enzyme from Rhodospirillum rubrum."; J. Bioenerg. Biomembr. 26:435-445(1994).
[2]	STRUCTURE BY NMR OF 262-464. DOI=10.1016/S0005-2728(00)00159-6; PubMed=11004437 [NCBI, ExPASy, EBI, Israel, Japan] Jeeves M., Smith K.J., Quirk P.G., Cotton N.P.J., Jackson J.B.; "Solution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from Rhodospirillum rubrum."; Biochim. Biophys. Acta 1459:248-257(2000).
[3]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 262-464. DOI=10.1016/S0969-2126(01)00571-8; PubMed=11250201 [NCBI, ExPASy, EBI, Israel, Japan] Cotton N.P.J., White S.A., Peake S.J., McSweeney S., Baz Jackson J.; "The crystal structure of an asymmetric complex of the two nucleotide binding components of proton-translocating transhydrogenase."; Structure 9:165-176(2001).

Comments

FUNCTION: The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane (By similarity).
CATALYTIC ACTIVITY: NADPH + NAD⁺ = NADP⁺ + NADH.
SUBUNIT: Complex of an alpha and a beta chain; in Rhodospirillum, the alpha chain seems to be made of two subunits.
SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein (By similarity).
SIMILARITY: Belongs to the PNT beta subunit 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

U01158; AAC43257.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

2FR8; X-ray; 2.60 A; C=262-464.	[ExPASy / RCSB / EBI]
2FRD; X-ray; 3.20 A; C=262-464.	[ExPASy / RCSB / EBI]
2FSV; X-ray; 2.30 A; C=262-464.	[ExPASy / RCSB / EBI]
2OO5; X-ray; 2.60 A; C=291-464.	[ExPASy / RCSB / EBI]
2OOR; X-ray; 2.32 A; C=291-464.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2FR8; -.
2FRD; -.
2FSV; -.
2OO5; -.
2OOR; -.

ModBase

P0C188.

Ontologies

GO:0055114;	Biological process: oxidation reduction (non-traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR012136; NADH_DH_b.
IPR004003; NADP_transhyd_b.
Graphical view of domain structure.

Pfam

PF02233; PNTB; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000204; PNTB; 1.

Other

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

Keywords

3D-structure; Cell inner membrane; Cell membrane; Membrane; NAD; NADP; Oxidoreductase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 464`	`464`	`NAD(P) transhydrogenase subunit beta.`	`PRO_0000199027`
`TRANSMEM`	`54 74`	`21`	`Potential.`
`TRANSMEM`	`86 106`	`21`	`Potential.`
`TRANSMEM`	`126 146`	`21`	`Potential.`
`TRANSMEM`	`164 184`	`21`	`Potential.`
`TRANSMEM`	`191 211`	`21`	`Potential.`
`TRANSMEM`	`227 247`	`21`	`Potential.`
`HELIX`	`297 306`	`10`
`STRAND`	`308 314`	`7`
`HELIX`	`316 321`	`6`
`HELIX`	`324 336`	`13`
`STRAND`	`340 345`	`6`
`STRAND`	`350 352`	`3`
`HELIX`	`355 362`	`8`
`HELIX`	`367 369`	`3`
`STRAND`	`370 372`	`3`
`HELIX`	`373 376`	`4`
`HELIX`	`377 379`	`3`
`STRAND`	`384 390`	`7`
`HELIX`	`393 395`	`3`
`HELIX`	`397 399`	`3`
`TURN`	`406 409`	`4`
`HELIX`	`415 417`	`3`
`STRAND`	`418 428`	`11`
`HELIX`	`438 441`	`4`
`STRAND`	`445 450`	`6`
`HELIX`	`452 462`	`11`

Sequence information

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

Molecular weight: 47808 Da [This is the MW of the unprocessed precursor]

CRC64: 79200D4F8861779B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTHSLTMAAY IVAGVLFILA LRGLSNPESA RNGNRMGMVG MAIAILTTLL SPSVQAYAWI 

        70         80         90        100        110        120 
VLAIAIGGAI GTVIAKKVLM TALPQLVAAF HSLVGMAAVL VATGALLNPE AYGIGSAGAI 

       130        140        150        160        170        180 
HAGSLVEMSL GLAVGAITFS GSVIAFGKLQ GLIAGKPVTF PMQHPLNAVL GILLVVLLVV 

       190        200        210        220        230        240 
FAATESHTAY FALMILAFAL GFLLIIPIGG ADMPVVISML NSYSGWAAAG IGFTLGNPLL 

       250        260        270        280        290        300 
IIAGALVGSS GAILSYIMCK GMNRSIFNVI LGGFGSEGGV AAAGGAAGDR SVKAGSAEDA 

       310        320        330        340        350        360 
AFIMKNASKV IIVPGYGMAV AQAQHALREM ADVLKKEGVE VSYAIHPVAG RMPGHMNVLL 

       370        380        390        400        410        420 
AEANVPYDEV FELEEINSSF QTADVAFVIG ANDVTNPAAK TDPSSPIYGM PILDVEKAGT 

       430        440        450        460 
VLFIKRSMAS GYAGVENELF FRNNTMMLFG DAKKMTEQIV QAMN

P0C188 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