ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P07001


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PNTA_ECOLI
Primary accession number P07001
Secondary accession number P76888
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on April 1, 1993 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 94)
Name and origin of the protein
Protein name NAD(P) transhydrogenase subunit alpha
Synonyms EC 1.6.1.2
Nicotinamide nucleotide transhydrogenase subunit alpha
Pyridine nucleotide transhydrogenase subunit alpha
Gene name
Name: pntA
OrderedLocusNames: b1603, JW1595
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3525165 [NCBI, ExPASy, EBI, Israel, Japan]
Clarke D.M., Loo T.W., Gillam S., Bragg P.D.;
"Nucleotide sequence of the pntA and pntB genes encoding the pyridine nucleotide transhydrogenase of Escherichia coli.";
Eur. J. Biochem. 158:647-653(1986).
[2]
SEQUENCE REVISION.
PubMed=1633824 [NCBI, ExPASy, EBI, Israel, Japan]
Ahmad S., Glavas N.A., Bragg P.D.;
"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.";
Eur. J. Biochem. 207:733-739(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.6.363; PubMed=9097039 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"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.";
DNA Res. 3:363-377(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
PROTEIN SEQUENCE OF 1-10; 16-25; 229-238 AND 270-285.
DOI=10.1016/0167-4838(91)90106-A; PubMed=1932078 [NCBI, ExPASy, EBI, Israel, Japan]
Tong R.C., Glavas N.A., Bragg P.D.;
"Topological analysis of the pyridine nucleotide transhydrogenase of Escherichia coli using proteolytic enzymes.";
Biochim. Biophys. Acta 1080:19-28(1991).
[7]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.1109730; PubMed=15919996 [NCBI, ExPASy, EBI, Israel, Japan]
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane proteome.";
Science 308:1321-1323(2005).
[8]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-394.
DOI=10.1016/j.jmb.2005.07.022; PubMed=16083909 [NCBI, ExPASy, EBI, Israel, Japan]
Johansson T., Oswald C., Pedersen A., Toernroeth S., Okvist M., Karlsson B.G., Rydstroem J., Krengel U.;
"X-ray structure of domain I of the proton-pumping membrane protein transhydrogenase from Escherichia coli.";
J. Mol. Biol. 352:299-312(2005).
Comments
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
X04195; CAB37089.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X66086; CAA46884.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC74675.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA15342.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S24380; DEECXA.
RefSeq AP_002224.1; -.
NP_416120.1; -.
3D structure databases
PDB
1X13; X-ray; 1.90 A; A/B=2-394.[ExPASy / RCSB / EBI]
1X14; X-ray; 1.94 A; A/B=2-394.[ExPASy / RCSB / EBI]
1X15; X-ray; 2.04 A; A/B=2-394.[ExPASy / RCSB / EBI]
2BRU; NMR; -; A/B=2-394.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1X13; -.
1X14; -.
1X15; -.
2BRU; -.
ModBase P07001.
Protein-protein interaction databases
DIP DIP:366N; -.
Enzyme and pathway databases
BioCyc EcoCyc:PNTA-MON; -.
MetaCyc:PNTA-MON; -.
Organism-specific databases
EchoBASE EB0737; -.
EcoGene EG10744; pntA.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.
IPR004571; NADP_transhyd_a.
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.
TIGRFAMs TIGR00561; pntA; 1.
PROSITE PS00836; ALADH_PNT_1; 1.
PS00837; ALADH_PNT_2; 1.
BLOCKS P07001.
ProtoNet P07001.
Genome annotation databases
GeneID 946628; -.
GenomeReviews U00096_GR; b1603.
AP009048_GR; JW1595.
KEGG ecj:JW1595; -.
eco:b1603; -.
Phylogenomic databases
HOGENOM P07001; -.
Other
LinkHub P07001; -.
Genome annotation databases
CMR P07001; b1603.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell inner membrane; Cell membrane; Complete proteome; Direct protein sequencing; Membrane; NAD; NADP; Oxidoreductase; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   510  510     NAD(P) transhydrogenase subunit alpha. PRO_0000199017
TOPO_DOM   1   401  401     Cytoplasmic (Potential). 
TRANSMEM   402   422  21     Potential. 
TRANSMEM   423   443  21     Potential. 
TOPO_DOM   444   452  9     Cytoplasmic (Potential). 
TRANSMEM   453   473  21     Potential. 
TOPO_DOM   474   476  3     Periplasmic (Potential). 
TRANSMEM   477   497  21     Potential. 
TOPO_DOM   498   510  13     Cytoplasmic (Potential). 
NP_BIND   167   197  31     NAD (By similarity). 
STRAND   2     5  4      
HELIX   20    28  9      
STRAND   32    36  5      
TURN   37    40  4      
HELIX   41    43  3      
HELIX   47    53  7      
STRAND   56    58  3      
HELIX   60    64  5      
STRAND   65    70  6      
HELIX   77    80  4      
STRAND   88    91  4      
HELIX   95    97  3      
HELIX   99   107  9      
STRAND   111   114  4      
HELIX   115   117  3      
HELIX   122   127  6      
HELIX   129   148  20      
STRAND   156   158  3      
STRAND   161   163  3      
STRAND   167   171  5      
HELIX   175   186  12      
STRAND   190   194  5      
HELIX   198   200  3      
HELIX   201   206  6      
HELIX   225   230  6      
HELIX   232   248  17      
STRAND   250   254  5      
HELIX   269   273  5      
STRAND   280   283  4      
HELIX   286   288  3      
STRAND   299   302  4      
STRAND   308   310  3      
HELIX   316   318  3      
HELIX   320   338  19      
STRAND   341   344  4      
HELIX   353   358  6      
STRAND   359   362  4      
Sequence information
Length: 510 AA [This is the length of the unprocessed precursor] Molecular weight: 54623 Da [This is the MW of the unprocessed precursor] CRC64: 801742097BEA6943 [This is a checksum on the sequence]
        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 

P07001 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 logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!