EC 1.6.1.2
Nicotinamide nucleotide transhydrogenase subunit alpha 1
Pyridine nucleotide transhydrogenase subunit alpha 1
Proton-translocating transhydrogenase component 1
dI

Gene name

	Name:	pntAA
	Synonyms:	nntA1

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]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). DOI=10.1016/S0969-2126(00)00171-4; PubMed=10997900 [NCBI, ExPASy, EBI, Israel, Japan] Buckley P.A., Jackson J.B., Schneider T., White S.A., Rice D.W., Baker P.J.; "Protein-protein recognition, hydride transfer and proton pumping in the transhydrogenase complex."; Structure 8:809-815(2000).
[3]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). 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.
SIMILARITY: Belongs to the AlaDH/PNT 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; AAC43255.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S69123; S69123.

3D structure databases

PDB

2FR8; X-ray; 2.60 A; A/B=1-384.	[ExPASy / RCSB / EBI]
2FRD; X-ray; 3.20 A; A/B=1-384.	[ExPASy / RCSB / EBI]
2FSV; X-ray; 2.30 A; A/B=1-384.	[ExPASy / RCSB / EBI]
2OO5; X-ray; 2.60 A; A/B=1-384.	[ExPASy / RCSB / EBI]
2OOR; X-ray; 2.32 A; A/B=1-384.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

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

ModBase

P0C186.

Ontologies

GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0008750;	Molecular function: NAD(P)+ transhydrogenase (AB-specific) activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (non-traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR007698; Ala_DHase/PNT_C.
IPR008142; Ala_DHase/PNT_CS1.
IPR008143; Ala_DHase/PNT_CS2.
IPR007886; Ala_DHase/PNT_N.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF01262; AlaDh_PNT_C; 1.
PF05222; AlaDh_PNT_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS00836; ALADH_PNT_1; 1.
PS00837; ALADH_PNT_2; 1.

Other

P0C186; -.

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

Keywords

3D-structure; NAD; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 384`	`384`	`NAD(P) transhydrogenase subunit alpha part 1.`	`PRO_0000199019`
`NP_BIND`	`167 197`	`31`	`NAD (By similarity).`
`STRAND`	`2 5`	`4`
`HELIX`	`20 29`	`10`
`STRAND`	`32 36`	`5`
`TURN`	`37 44`	`8`
`HELIX`	`47 52`	`6`
`STRAND`	`55 60`	`6`
`HELIX`	`61 65`	`5`
`STRAND`	`69 72`	`4`
`HELIX`	`80 82`	`3`
`HELIX`	`87 89`	`3`
`STRAND`	`95 98`	`4`
`TURN`	`102 104`	`3`
`HELIX`	`106 114`	`9`
`STRAND`	`118 121`	`4`
`HELIX`	`122 124`	`3`
`HELIX`	`129 134`	`6`
`HELIX`	`136 155`	`20`
`STRAND`	`163 165`	`3`
`STRAND`	`168 170`	`3`
`STRAND`	`174 178`	`5`
`HELIX`	`182 193`	`12`
`STRAND`	`197 201`	`5`
`HELIX`	`207 213`	`7`
`HELIX`	`241 255`	`15`
`STRAND`	`259 263`	`5`
`HELIX`	`278 282`	`5`
`STRAND`	`289 292`	`4`
`HELIX`	`295 297`	`3`
`STRAND`	`308 312`	`5`
`STRAND`	`315 319`	`5`
`HELIX`	`323 327`	`5`
`HELIX`	`328 343`	`16`
`HELIX`	`344 346`	`3`
`TURN`	`349 352`	`4`
`HELIX`	`361 366`	`6`
`STRAND`	`367 370`	`4`

Sequence information

Length: 384 AA [This is the length of the unprocessed precursor]

Molecular weight: 40277 Da [This is the MW of the unprocessed precursor]

CRC64: B886A640CE2BFA12 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKIAIPKERR PGEDRVAISP EVVKKLVGLG FEVIVEQGAG VGASITDDAL TAAGATIAST 

        70         80         90        100        110        120 
AAQALSQADV VWKVQRPMTA EEGTDEVALI KEGAVLMCHL GALTNRPVVE ALTKRKITAY 

       130        140        150        160        170        180 
AMELMPRISR AQSMDILSSQ SNLAGYRAVI DGAYEFARAF PMMMTAAGTV PPARVLVFGV 

       190        200        210        220        230        240 
GVAGLQAIAT AKRLGAVVMA TDVRAATKEQ VESLGGKFIT VDDEAMKTAE TAGGYAKEMG 

       250        260        270        280        290        300 
EEFRKKQAEA VLKELVKTDI AITTALIPGK PAPVLITEEM VTKMKPGSVI IDLAVEAGGN 

       310        320        330        340        350        360 
CPLSEPGKIV VKHGVKIVGH TNVPSRVAAD ASPLFAKNLL NFLTPHVDKD TKTLVMKLED 

       370        380 
ETVSGTCVTR DGAIVHPALT GQGA

P0C186 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