PNTA_HAEIN
ID PNTA_HAEIN Reviewed; 512 AA.
AC P43842;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=NAD(P) transhydrogenase subunit alpha;
DE EC=7.1.1.1 {ECO:0000250|UniProtKB:P07001};
DE AltName: Full=Nicotinamide nucleotide transhydrogenase subunit alpha;
DE AltName: Full=Pyridine nucleotide transhydrogenase subunit alpha;
GN Name=pntA; OrderedLocusNames=HI_1362;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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:0000250}.
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:0000250|UniProtKB:P07001};
CC -!- SUBUNIT: Heterodimer of an alpha (PntA) and a beta (PntB) chain.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family. {ECO:0000305}.
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DR EMBL; L42023; AAC23009.1; -; Genomic_DNA.
DR PIR; E64119; E64119.
DR RefSeq; NP_439513.1; NC_000907.1.
DR RefSeq; WP_005693998.1; NC_000907.1.
DR AlphaFoldDB; P43842; -.
DR SMR; P43842; -.
DR STRING; 71421.HI_1362; -.
DR PRIDE; P43842; -.
DR EnsemblBacteria; AAC23009; AAC23009; HI_1362.
DR KEGG; hin:HI_1362; -.
DR PATRIC; fig|71421.8.peg.1416; -.
DR eggNOG; COG3288; Bacteria.
DR HOGENOM; CLU_003376_2_1_6; -.
DR OMA; YFPMLMT; -.
DR PhylomeDB; P43842; -.
DR BioCyc; HINF71421:G1GJ1-1387-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; ISS: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; ISS:UniProtKB.
DR GO; GO:0006740; P:NADPH regeneration; IBA:GO_Central.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:InterPro.
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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; NAD; NADP;
KW Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..512
FT /note="NAD(P) transhydrogenase subunit alpha"
FT /id="PRO_0000199018"
FT TOPO_DOM 1..400
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..451
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..478
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 500..512
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 375..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 125..128
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 195..197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 512 AA; 54973 MW; 50D63AD536E837EF CRC64;
MLIGVPRELL ENESRVAATP KTVQQILKLG FDVIVEHDAG FKASFEDQAF LEAGAKIGTS
AEIWQSDIIF KVNAPTDEEI AQMKEGAALV SFIWRMQNPE LMKKLTAKKI NVLAMDAVPR
ISRAQALDAL SSMANISGYR AVIEAAHEFG SFFTGQITAA GKVPPAKVLV IGAGVAGLAA
IGAANSLGAI VRAFDSRPEV KEQVQSMGAS FLEIDFKEEG GSGDGYAKVM SEEFNRRAME
LYAEQAKEVD IIITTAAIPG KPAPRLITKE MVDSMKPGSV IVDLAAATGG NCEYTQAGKV
VTTENQVKVI GYTDFPSRLP TQSSQLYGTN LVNLLKLLCK EKDGNINIDF EDVVLRGVTV
VRDGEEIPPA QIQVSAQPKQ ETKAAPVAEK KESKPTDPRV KYGVMAGVGV LFLWLASVAP
AAFLSHFTVF VLACVVGYYV VWNVSHALHT PLMAVTNAIS GIIIVGALLQ IRQPTGNLFI
DALAFVAILV ASINIFGGFR VTQRMLAMFR KG
