PNTA_ECOLI
ID PNTA_ECOLI Reviewed; 510 AA.
AC P07001; P76888;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=NAD(P) transhydrogenase subunit alpha;
DE EC=7.1.1.1 {ECO:0000269|PubMed:16083909};
DE AltName: Full=Nicotinamide nucleotide transhydrogenase subunit alpha;
DE AltName: Full=Pyridine nucleotide transhydrogenase subunit alpha;
GN Name=pntA; OrderedLocusNames=b1603, JW1595;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3525165; DOI=10.1111/j.1432-1033.1986.tb09802.x;
RA Clarke D.M., Loo T.W., Gillam S., Bragg P.D.;
RT "Nucleotide sequence of the pntA and pntB genes encoding the pyridine
RT nucleotide transhydrogenase of Escherichia coli.";
RL Eur. J. Biochem. 158:647-653(1986).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=1633824; DOI=10.1111/j.1432-1033.1992.tb17103.x;
RA Ahmad S., Glavas N.A., Bragg P.D.;
RT "A mutation at Gly314 of the beta subunit of the Escherichia coli pyridine
RT nucleotide transhydrogenase abolishes activity and affects the NADP(H)-
RT induced conformational change.";
RL Eur. J. Biochem. 207:733-739(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 1-10; 16-25; 229-238 AND 270-285.
RX PubMed=1932078; DOI=10.1016/0167-4838(91)90106-a;
RA Tong R.C., Glavas N.A., Bragg P.D.;
RT "Topological analysis of the pyridine nucleotide transhydrogenase of
RT Escherichia coli using proteolytic enzymes.";
RL Biochim. Biophys. Acta 1080:19-28(1991).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-394 OF APOENZYME AND IN
RP COMPLEXES WITH NAD AND NADH, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP CHARACTERIZATION OF MUTANT DEL 151-161.
RX PubMed=16083909; DOI=10.1016/j.jmb.2005.07.022;
RA Johansson T., Oswald C., Pedersen A., Toernroeth S., Okvist M.,
RA Karlsson B.G., Rydstroem J., Krengel U.;
RT "X-ray structure of domain I of the proton-pumping membrane protein
RT transhydrogenase from Escherichia coli.";
RL J. Mol. Biol. 352:299-312(2005).
RN [9]
RP STRUCTURE BY NMR OF 2-394 IN COMPLEX WITH NAD AND PNTB.
RA Johansson T., Pedersen A., Leckner J., Karlsson B.G.;
RT "Structure determination of a transient complex by NMR using paramagnetic
RT distance restraints - the complex of the soluble domains of Escherichia
RT coli transhydrogenase.";
RL Submitted (MAY-2005) to the PDB data bank.
CC -!- FUNCTION: The transhydrogenation between NADH and NADP is coupled to
CC respiration and ATP hydrolysis and functions as a proton pump across
CC the membrane. {ECO:0000269|PubMed:16083909}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + NAD(+) + NADPH = H(+)(out) + NADH + NADP(+);
CC Xref=Rhea:RHEA:47992, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57945, ChEBI:CHEBI:58349; EC=7.1.1.1;
CC Evidence={ECO:0000269|PubMed:16083909};
CC -!- SUBUNIT: Heterodimer of an alpha (PntA) and a beta (PntB) chain. Alpha
CC subunit serves as the dimerization unit. {ECO:0000269|PubMed:16083909,
CC ECO:0000269|Ref.9}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family. {ECO:0000305}.
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DR EMBL; X04195; CAB37089.1; -; Genomic_DNA.
DR EMBL; X66086; CAA46884.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74675.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15342.1; -; Genomic_DNA.
DR PIR; S24380; DEECXA.
DR RefSeq; NP_416120.1; NC_000913.3.
DR RefSeq; WP_001300486.1; NZ_SSZK01000001.1.
DR PDB; 1X13; X-ray; 1.90 A; A/B=2-394.
DR PDB; 1X14; X-ray; 1.94 A; A/B=2-394.
DR PDB; 1X15; X-ray; 2.04 A; A/B=2-394.
DR PDB; 2BRU; NMR; -; A/B=2-394.
DR PDBsum; 1X13; -.
DR PDBsum; 1X14; -.
DR PDBsum; 1X15; -.
DR PDBsum; 2BRU; -.
DR AlphaFoldDB; P07001; -.
DR SMR; P07001; -.
DR BioGRID; 4260811; 46.
DR BioGRID; 850974; 2.
DR ComplexPortal; CPX-5623; NAD(P) transhydrogenase complex.
DR DIP; DIP-366N; -.
DR IntAct; P07001; 2.
DR STRING; 511145.b1603; -.
DR TCDB; 3.D.2.1.1; the proton-translocating transhydrogenase (pth) family.
DR jPOST; P07001; -.
DR PaxDb; P07001; -.
DR PRIDE; P07001; -.
DR EnsemblBacteria; AAC74675; AAC74675; b1603.
DR EnsemblBacteria; BAA15342; BAA15342; BAA15342.
DR GeneID; 946628; -.
DR KEGG; ecj:JW1595; -.
DR KEGG; eco:b1603; -.
DR PATRIC; fig|1411691.4.peg.659; -.
DR EchoBASE; EB0737; -.
DR eggNOG; COG3288; Bacteria.
DR HOGENOM; CLU_003376_2_1_6; -.
DR InParanoid; P07001; -.
DR OMA; YFPMLMT; -.
DR PhylomeDB; P07001; -.
DR BioCyc; EcoCyc:PNTA-MON; -.
DR BioCyc; MetaCyc:PNTA-MON; -.
DR BRENDA; 1.6.1.2; 2026.
DR BRENDA; 7.1.1.1; 2026.
DR EvolutionaryTrace; P07001; -.
DR PRO; PR:P07001; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0009327; C:NAD(P)+ transhydrogenase complex (AB-specific); IPI:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0051287; F:NAD binding; IDA:EcoCyc.
DR GO; GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; IDA:UniProtKB.
DR GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IDA:UniProtKB.
DR GO; GO:0006740; P:NADPH regeneration; IDA:UniProtKB.
DR GO; GO:0120029; P:proton export across plasma membrane; IDA:ComplexPortal.
DR InterPro; IPR008143; Ala_DH/PNT_CS2.
DR InterPro; IPR008142; AlaDH/PNT_CS1.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR026255; NADP_transhyd_a.
DR InterPro; IPR024605; NADP_transhyd_a_C.
DR Pfam; PF01262; AlaDh_PNT_C; 1.
DR Pfam; PF05222; AlaDh_PNT_N; 1.
DR Pfam; PF12769; PNTB_4TM; 1.
DR PIRSF; PIRSF000203; NADP_transhydrogenase_alpha; 1.
DR SMART; SM01002; AlaDh_PNT_C; 1.
DR SMART; SM01003; AlaDh_PNT_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00561; pntA; 1.
DR PROSITE; PS00836; ALADH_PNT_1; 1.
DR PROSITE; PS00837; ALADH_PNT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Membrane; NAD; NADP; Nucleotide-binding;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..510
FT /note="NAD(P) transhydrogenase subunit alpha"
FT /id="PRO_0000199017"
FT TOPO_DOM 1..401
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..452
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..476
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 498..510
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 120..122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.9"
FT BINDING 175
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.9"
FT BINDING 195..197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.9"
FT BINDING 238
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.9"
FT BINDING 257
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.9"
FT MUTAGEN 151..161
FT /note="Missing: Dimerizes; affinity for PntB unchanged, but
FT maximum transhydrogenation rate lowered significantly."
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:1X13"
FT HELIX 20..28
FT /evidence="ECO:0007829|PDB:1X13"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:1X13"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:1X13"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1X13"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:1X13"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1X13"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:1X13"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:1X13"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:1X13"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:1X13"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1X13"
FT HELIX 99..107
FT /evidence="ECO:0007829|PDB:1X13"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:1X13"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:1X13"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:1X13"
FT HELIX 129..148
FT /evidence="ECO:0007829|PDB:1X13"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:1X13"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:1X13"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:1X13"
FT HELIX 175..186
FT /evidence="ECO:0007829|PDB:1X13"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:1X13"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:1X13"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:1X13"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:2BRU"
FT HELIX 225..230
FT /evidence="ECO:0007829|PDB:1X13"
FT HELIX 232..248
FT /evidence="ECO:0007829|PDB:1X13"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:1X13"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:2BRU"
FT HELIX 269..273
FT /evidence="ECO:0007829|PDB:1X13"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:1X13"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:1X13"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:2BRU"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:1X13"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:2BRU"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:1X13"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:1X13"
FT HELIX 320..338
FT /evidence="ECO:0007829|PDB:1X13"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:1X13"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:2BRU"
FT HELIX 353..358
FT /evidence="ECO:0007829|PDB:1X13"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:1X13"
SQ SEQUENCE 510 AA; 54623 MW; 801742097BEA6943 CRC64;
MRIGIPRERL TNETRVAATP KTVEQLLKLG FTVAVESGAG QLASFDDKAF VQAGAEIVEG
NSVWQSEIIL KVNAPLDDEI ALLNPGTTLV SFIWPAQNPE LMQKLAERNV TVMAMDSVPR
ISRAQSLDAL SSMANIAGYR AIVEAAHEFG RFFTGQITAA GKVPPAKVMV IGAGVAGLAA
IGAANSLGAI VRAFDTRPEV KEQVQSMGAE FLELDFKEEA GSGDGYAKVM SDAFIKAEME
LFAAQAKEVD IIVTTALIPG KPAPKLITRE MVDSMKAGSV IVDLAAQNGG NCEYTVPGEI
FTTENGVKVI GYTDLPGRLP TQSSQLYGTN LVNLLKLLCK EKDGNITVDF DDVVIRGVTV
IRAGEITWPA PPIQVSAQPQ AAQKAAPEVK TEEKCTCSPW RKYALMALAI ILFGWMASVA
PKEFLGHFTV FALACVVGYY VVWNVSHALH TPLMSVTNAI SGIIVVGALL QIGQGGWVSF
LSFIAVLIAS INIFGGFTVT QRMLKMFRKN
