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Protein

NAD(P) transhydrogenase subunit alpha

Gene

pntA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane.

Catalytic activityi

NADPH + NAD+ = NADP+ + NADH.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei175 – 1751NAD; via amide nitrogen1 Publication
Binding sitei238 – 2381NAD1 Publication
Binding sitei257 – 2571NAD; via carbonyl oxygen1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi120 – 1223NAD1 Publication
Nucleotide bindingi195 – 1973NAD1 Publication

GO - Molecular functioni

  • NAD(P)+ transhydrogenase (AB-specific) activity Source: UniProtKB
  • NAD binding Source: EcoCyc
  • NADP binding Source: GO_Central
  • protein dimerization activity Source: UniProtKB

GO - Biological processi

  • NADPH regeneration Source: UniProtKB
  • proton transport Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:PNTA-MONOMER.
ECOL316407:JW1595-MONOMER.
MetaCyc:PNTA-MONOMER.
BRENDAi1.6.1.2. 2026.

Protein family/group databases

TCDBi3.D.2.1.1. the proton-translocating transhydrogenase (pth) family.

Names & Taxonomyi

Protein namesi
Recommended name:
NAD(P) transhydrogenase subunit alpha (EC:1.6.1.2)
Alternative name(s):
Nicotinamide nucleotide transhydrogenase subunit alpha
Pyridine nucleotide transhydrogenase subunit alpha
Gene namesi
Name:pntA
Ordered Locus Names:b1603, JW1595
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10744. pntA.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 401401CytoplasmicSequence analysisAdd
BLAST
Transmembranei402 – 42221HelicalSequence analysisAdd
BLAST
Transmembranei423 – 44321HelicalSequence analysisAdd
BLAST
Topological domaini444 – 4529CytoplasmicSequence analysis
Transmembranei453 – 47321HelicalSequence analysisAdd
BLAST
Topological domaini474 – 4763PeriplasmicSequence analysis
Transmembranei477 – 49721HelicalSequence analysisAdd
BLAST
Topological domaini498 – 51013CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: UniProtKB
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi151 – 16111Missing : Dimerizes; affinity for PntB unchanged, but maximum transhydrogenation rate lowered significantly. Add
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 510510NAD(P) transhydrogenase subunit alphaPRO_0000199017Add
BLAST

Proteomic databases

EPDiP07001.
PaxDbiP07001.
PRIDEiP07001.

Interactioni

Subunit structurei

Heterodimer of an alpha (PntA) and a beta (PntB) chain. Alpha subunit serves as the dimerization unit.2 Publications

GO - Molecular functioni

  • protein dimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi4260811. 6 interactions.
DIPiDIP-366N.
IntActiP07001. 2 interactions.
MINTiMINT-1299705.
STRINGi511145.b1603.

Structurei

Secondary structure

1
510
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Helixi20 – 289Combined sources
Beta strandi32 – 365Combined sources
Turni37 – 404Combined sources
Helixi41 – 433Combined sources
Helixi47 – 537Combined sources
Beta strandi56 – 583Combined sources
Helixi60 – 645Combined sources
Beta strandi65 – 706Combined sources
Helixi77 – 804Combined sources
Beta strandi88 – 914Combined sources
Helixi95 – 973Combined sources
Helixi99 – 1079Combined sources
Beta strandi111 – 1144Combined sources
Helixi115 – 1173Combined sources
Helixi122 – 1276Combined sources
Helixi129 – 14820Combined sources
Beta strandi156 – 1583Combined sources
Beta strandi161 – 1633Combined sources
Beta strandi167 – 1715Combined sources
Helixi175 – 18612Combined sources
Beta strandi190 – 1945Combined sources
Helixi198 – 2003Combined sources
Helixi201 – 2066Combined sources
Beta strandi209 – 2113Combined sources
Helixi225 – 2306Combined sources
Helixi232 – 24817Combined sources
Beta strandi250 – 2545Combined sources
Beta strandi259 – 2613Combined sources
Helixi269 – 2735Combined sources
Beta strandi280 – 2834Combined sources
Helixi286 – 2883Combined sources
Beta strandi291 – 2944Combined sources
Beta strandi299 – 3024Combined sources
Turni304 – 3063Combined sources
Beta strandi308 – 3103Combined sources
Helixi316 – 3183Combined sources
Helixi320 – 33819Combined sources
Beta strandi341 – 3444Combined sources
Beta strandi350 – 3523Combined sources
Helixi353 – 3586Combined sources
Beta strandi359 – 3624Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X13X-ray1.90A/B2-394[»]
1X14X-ray1.94A/B2-394[»]
1X15X-ray2.04A/B2-394[»]
2BRUNMR-A/B2-394[»]
ProteinModelPortaliP07001.
SMRiP07001. Positions 2-372.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07001.

Family & Domainsi

Sequence similaritiesi

Belongs to the AlaDH/PNT family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4108IIE. Bacteria.
COG3288. LUCA.
HOGENOMiHOG000022121.
InParanoidiP07001.
KOiK00324.
OMAiNVAPKEF.
OrthoDBiEOG61P6S9.
PhylomeDBiP07001.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
InterProiIPR008143. Ala_DH/PNT_CS2.
IPR008142. AlaDH/PNT_CS1.
IPR007886. AlaDH/PNT_N.
IPR007698. AlaDH/PNT_NAD(H)-bd.
IPR023753. FAD/NAD-binding_dom.
IPR016040. NAD(P)-bd_dom.
IPR026255. NADP_transhyd_a.
IPR024605. NADP_transhyd_a_C.
[Graphical view]
PfamiPF01262. AlaDh_PNT_C. 1 hit.
PF05222. AlaDh_PNT_N. 1 hit.
PF12769. PNTB_4TM. 1 hit.
[Graphical view]
PIRSFiPIRSF000203. NADP_transhydrogenase_alpha. 1 hit.
SMARTiSM01002. AlaDh_PNT_C. 1 hit.
SM01003. AlaDh_PNT_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00561. pntA. 1 hit.
PROSITEiPS00836. ALADH_PNT_1. 1 hit.
PS00837. ALADH_PNT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07001-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRIGIPRERL TNETRVAATP KTVEQLLKLG FTVAVESGAG QLASFDDKAF
60 70 80 90 100
VQAGAEIVEG NSVWQSEIIL KVNAPLDDEI ALLNPGTTLV SFIWPAQNPE
110 120 130 140 150
LMQKLAERNV TVMAMDSVPR ISRAQSLDAL SSMANIAGYR AIVEAAHEFG
160 170 180 190 200
RFFTGQITAA GKVPPAKVMV IGAGVAGLAA IGAANSLGAI VRAFDTRPEV
210 220 230 240 250
KEQVQSMGAE FLELDFKEEA GSGDGYAKVM SDAFIKAEME LFAAQAKEVD
260 270 280 290 300
IIVTTALIPG KPAPKLITRE MVDSMKAGSV IVDLAAQNGG NCEYTVPGEI
310 320 330 340 350
FTTENGVKVI GYTDLPGRLP TQSSQLYGTN LVNLLKLLCK EKDGNITVDF
360 370 380 390 400
DDVVIRGVTV IRAGEITWPA PPIQVSAQPQ AAQKAAPEVK TEEKCTCSPW
410 420 430 440 450
RKYALMALAI ILFGWMASVA PKEFLGHFTV FALACVVGYY VVWNVSHALH
460 470 480 490 500
TPLMSVTNAI SGIIVVGALL QIGQGGWVSF LSFIAVLIAS INIFGGFTVT
510
QRMLKMFRKN
Length:510
Mass (Da):54,623
Last modified:April 1, 1993 - v2
Checksum:i801742097BEA6943
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04195 Genomic DNA. Translation: CAB37089.1.
X66086 Genomic DNA. Translation: CAA46884.1.
U00096 Genomic DNA. Translation: AAC74675.1.
AP009048 Genomic DNA. Translation: BAA15342.1.
PIRiS24380. DEECXA.
RefSeqiNP_416120.1. NC_000913.3.
WP_001300486.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74675; AAC74675; b1603.
BAA15342; BAA15342; BAA15342.
GeneIDi946628.
KEGGiecj:JW1595.
eco:b1603.
PATRICi32118508. VBIEscCol129921_1674.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04195 Genomic DNA. Translation: CAB37089.1.
X66086 Genomic DNA. Translation: CAA46884.1.
U00096 Genomic DNA. Translation: AAC74675.1.
AP009048 Genomic DNA. Translation: BAA15342.1.
PIRiS24380. DEECXA.
RefSeqiNP_416120.1. NC_000913.3.
WP_001300486.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X13X-ray1.90A/B2-394[»]
1X14X-ray1.94A/B2-394[»]
1X15X-ray2.04A/B2-394[»]
2BRUNMR-A/B2-394[»]
ProteinModelPortaliP07001.
SMRiP07001. Positions 2-372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260811. 6 interactions.
DIPiDIP-366N.
IntActiP07001. 2 interactions.
MINTiMINT-1299705.
STRINGi511145.b1603.

Protein family/group databases

TCDBi3.D.2.1.1. the proton-translocating transhydrogenase (pth) family.

Proteomic databases

EPDiP07001.
PaxDbiP07001.
PRIDEiP07001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74675; AAC74675; b1603.
BAA15342; BAA15342; BAA15342.
GeneIDi946628.
KEGGiecj:JW1595.
eco:b1603.
PATRICi32118508. VBIEscCol129921_1674.

Organism-specific databases

EchoBASEiEB0737.
EcoGeneiEG10744. pntA.

Phylogenomic databases

eggNOGiENOG4108IIE. Bacteria.
COG3288. LUCA.
HOGENOMiHOG000022121.
InParanoidiP07001.
KOiK00324.
OMAiNVAPKEF.
OrthoDBiEOG61P6S9.
PhylomeDBiP07001.

Enzyme and pathway databases

BioCyciEcoCyc:PNTA-MONOMER.
ECOL316407:JW1595-MONOMER.
MetaCyc:PNTA-MONOMER.
BRENDAi1.6.1.2. 2026.

Miscellaneous databases

EvolutionaryTraceiP07001.
PROiP07001.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
InterProiIPR008143. Ala_DH/PNT_CS2.
IPR008142. AlaDH/PNT_CS1.
IPR007886. AlaDH/PNT_N.
IPR007698. AlaDH/PNT_NAD(H)-bd.
IPR023753. FAD/NAD-binding_dom.
IPR016040. NAD(P)-bd_dom.
IPR026255. NADP_transhyd_a.
IPR024605. NADP_transhyd_a_C.
[Graphical view]
PfamiPF01262. AlaDh_PNT_C. 1 hit.
PF05222. AlaDh_PNT_N. 1 hit.
PF12769. PNTB_4TM. 1 hit.
[Graphical view]
PIRSFiPIRSF000203. NADP_transhydrogenase_alpha. 1 hit.
SMARTiSM01002. AlaDh_PNT_C. 1 hit.
SM01003. AlaDh_PNT_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00561. pntA. 1 hit.
PROSITEiPS00836. ALADH_PNT_1. 1 hit.
PS00837. ALADH_PNT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the pntA and pntB genes encoding the pyridine nucleotide transhydrogenase of Escherichia coli."
    Clarke D.M., Loo T.W., Gillam S., Bragg P.D.
    Eur. J. Biochem. 158:647-653(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "A mutation at Gly314 of the beta subunit of the Escherichia coli pyridine nucleotide transhydrogenase abolishes activity and affects the NADP(H)-induced conformational change."
    Ahmad S., Glavas N.A., Bragg P.D.
    Eur. J. Biochem. 207:733-739(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Topological analysis of the pyridine nucleotide transhydrogenase of Escherichia coli using proteolytic enzymes."
    Tong R.C., Glavas N.A., Bragg P.D.
    Biochim. Biophys. Acta 1080:19-28(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-10; 16-25; 229-238 AND 270-285.
  7. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.
  8. "X-ray structure of domain I of the proton-pumping membrane protein transhydrogenase from Escherichia coli."
    Johansson T., Oswald C., Pedersen A., Toernroeth S., Okvist M., Karlsson B.G., Rydstroem J., Krengel U.
    J. Mol. Biol. 352:299-312(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-394 OF APOENZYME AND IN COMPLEXES WITH NAD AND NADH, CATALYTIC ACTIVITY, SUBUNIT, CHARACTERIZATION OF MUTANT DEL 151-161.
  9. "Structure determination of a transient complex by NMR using paramagnetic distance restraints - the complex of the soluble domains of Escherichia coli transhydrogenase."
    Johansson T., Pedersen A., Leckner J., Karlsson B.G.
    Submitted (MAY-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 2-394 IN COMPLEX WITH NAD AND PNTB.

Entry informationi

Entry nameiPNTA_ECOLI
AccessioniPrimary (citable) accession number: P07001
Secondary accession number(s): P76888
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1993
Last modified: March 16, 2016
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.