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Reviewed, UniProtKB/Swiss-Prot P07001 (PNTA_ECOLI)

Last modified June 16, 2009. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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 names
Name: pntA
Ordered Locus Names: b1603, JW1595
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length510 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

Catalytic activity

NADPH + NAD+ = NADP+ + NADH.

Subunit structure

Heterodimer of an alpha and a beta chain.

Subcellular location

Cell inner membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the AlaDH/PNT family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 510510NAD(P) transhydrogenase subunit alpha
PRO_0000199017

Regions

Topological domain1 – 401401Cytoplasmic Potential
Transmembrane402 – 42221 Potential
Transmembrane423 – 44321 Potential
Topological domain444 – 4529Cytoplasmic Potential
Transmembrane453 – 47321 Potential
Topological domain474 – 4763Periplasmic Potential
Transmembrane477 – 49721 Potential
Topological domain498 – 51013Cytoplasmic Potential
Nucleotide binding167 – 19731NAD By similarity

Secondary structure

..................................................................... 510
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07001-1 [UniParc].

Last modified April 1, 1993. Version 2.
Checksum: 801742097BEA6943

FASTA51054,623
        10         20         30         40         50         60 
MRIGIPRERL TNETRVAATP KTVEQLLKLG FTVAVESGAG QLASFDDKAF VQAGAEIVEG 

        70         80         90        100        110        120 
NSVWQSEIIL KVNAPLDDEI ALLNPGTTLV SFIWPAQNPE LMQKLAERNV TVMAMDSVPR 

       130        140        150        160        170        180 
ISRAQSLDAL SSMANIAGYR AIVEAAHEFG RFFTGQITAA GKVPPAKVMV IGAGVAGLAA 

       190        200        210        220        230        240 
IGAANSLGAI VRAFDTRPEV KEQVQSMGAE FLELDFKEEA GSGDGYAKVM SDAFIKAEME 

       250        260        270        280        290        300 
LFAAQAKEVD IIVTTALIPG KPAPKLITRE MVDSMKAGSV IVDLAAQNGG NCEYTVPGEI 

       310        320        330        340        350        360 
FTTENGVKVI GYTDLPGRLP TQSSQLYGTN LVNLLKLLCK EKDGNITVDF DDVVIRGVTV 

       370        380        390        400        410        420 
IRAGEITWPA PPIQVSAQPQ AAQKAAPEVK TEEKCTCSPW RKYALMALAI ILFGWMASVA 

       430        440        450        460        470        480 
PKEFLGHFTV FALACVVGYY VVWNVSHALH TPLMSVTNAI SGIIVVGALL QIGQGGWVSF 

       490        500        510 
LSFIAVLIAS INIFGGFTVT QRMLKMFRKN 

« Hide

References

« Hide 'large scale' references
[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: 3525165] [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: 1633824] [Abstract]
Cited for: SEQUENCE REVISION.
[3]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
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: 16738553] [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: 1932078] [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: 15919996] [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: 16083909] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-394.

Cross-references

Sequence databases

X04195 Genomic DNA. Translation: CAB37089.1.
X66086 Genomic DNA. Translation: CAA46884.1.
U00096 Genomic DNA. Translation: AAC74675.1.
AP009048 Genomic DNA. Translation: BAA15342.1.
PIRDEECXA. S24380.
RefSeqAP_002224.1.
NP_416120.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1X13X-ray1.90A/B2-394[»]
1X14X-ray1.94A/B2-394[»]
1X15X-ray2.04A/B2-394[»]
2BRUNMR-A/B2-394[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:366N.

Protein family/group databases

TCDB3.D.2.1.1. proton-translocating transhydrogenase (PTH) family.

Genome annotation databases

GeneID946628.
GenomeReviewsGene locus JW1595 in contig AP009048_GR.
Gene locus b1603 in contig U00096_GR.
KEGGecj:JW1595.
eco:b1603.

Organism-specific databases

EchoBASEEB0737.
EcoGeneEG10744. pntA.
CMRSearch...

Phylogenomic databases

HOGENOMP07001.
OMAP07001. FKVNAPT.

Enzyme and pathway databases

BioCycEcoCyc:PNTA-MON.
MetaCyc:PNTA-MON.

Family and domain databases

InterProIPR007698. Ala_DH/PNT_C.
IPR008142. Ala_DH/PNT_CS1.
IPR008143. Ala_DH/PNT_CS2.
IPR007886. Ala_DH/PNT_N.
IPR016040. NAD(P)-bd_dom.
IPR004571. NADP_transhyd_a.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF01262. AlaDh_PNT_C. 1 hit.
PF05222. AlaDh_PNT_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR00561. pntA. 1 hit.
PROSITEPS00836. ALADH_PNT_1. 1 hit.
PS00837. ALADH_PNT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePNTA_ECOLI
AccessionPrimary (citable) accession number: P07001
Secondary accession number(s): P76888
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1993
Last modified: June 16, 2009
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents