ID   PNTAA_RHORU             Reviewed;         384 AA.
AC   P0C186; Q60164;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=NAD(P) transhydrogenase subunit alpha part 1;
DE            EC=7.1.1.1 {ECO:0000250|UniProtKB:Q2RSB2};
DE   AltName: Full=Nicotinamide nucleotide transhydrogenase subunit alpha 1;
DE   AltName: Full=Proton-translocating transhydrogenase component 1;
DE   AltName: Full=Pyridine nucleotide transhydrogenase subunit alpha 1;
DE   AltName: Full=dI;
GN   Name=pntAA; Synonyms=nntA1;
OS   Rhodospirillum rubrum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=1085;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7844118; DOI=10.1007/bf00762784;
RA   Yamaguchi M., Hatefi Y.;
RT   "Energy-transducing nicotinamide nucleotide transhydrogenase: nucleotide
RT   sequences of the genes and predicted amino acid sequences of the subunits
RT   of the enzyme from Rhodospirillum rubrum.";
RL   J. Bioenerg. Biomembr. 26:435-445(1994).
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:Q2RSB2};
CC   -!- SUBUNIT: Heterotrimer of two alpha chains and a beta (PntB) chain; in
CC       Rhodospirillum, the alpha chain is made of two subunits (PntAA and
CC       PntAB) and forms a dimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AlaDH/PNT family. {ECO:0000305}.
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DR   EMBL; U01158; AAC43255.1; -; Genomic_DNA.
DR   PIR; S69123; S69123.
DR   RefSeq; WP_011390032.1; NZ_NHSM01000143.1.
DR   AlphaFoldDB; P0C186; -.
DR   SMR; P0C186; -.
DR   TCDB; 3.D.2.2.1; the proton-translocating transhydrogenase (pth) family.
DR   EvolutionaryTrace; P0C186; -.
DR   GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
DR   GO; GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; ISS:UniProtKB.
DR   GO; GO:0070403; F:NAD+ binding; ISS:UniProtKB.
DR   GO; GO:0070404; F:NADH binding; ISS:UniProtKB.
DR   GO; GO:0006740; P:NADPH regeneration; ISS:UniProtKB.
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   Pfam; PF01262; AlaDh_PNT_C; 1.
DR   Pfam; PF05222; AlaDh_PNT_N; 1.
DR   SMART; SM01002; AlaDh_PNT_C; 1.
DR   SMART; SM01003; AlaDh_PNT_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00836; ALADH_PNT_1; 1.
DR   PROSITE; PS00837; ALADH_PNT_2; 1.
PE   3: Inferred from homology;
KW   NAD; NADP; Nucleotide-binding; Translocase.
FT   CHAIN           1..384
FT                   /note="NAD(P) transhydrogenase subunit alpha part 1"
FT                   /id="PRO_0000199019"
FT   BINDING         132..135
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         202..204
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         234
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   384 AA;  40277 MW;  B886A640CE2BFA12 CRC64;
     MKIAIPKERR PGEDRVAISP EVVKKLVGLG FEVIVEQGAG VGASITDDAL TAAGATIAST
     AAQALSQADV VWKVQRPMTA EEGTDEVALI KEGAVLMCHL GALTNRPVVE ALTKRKITAY
     AMELMPRISR AQSMDILSSQ SNLAGYRAVI DGAYEFARAF PMMMTAAGTV PPARVLVFGV
     GVAGLQAIAT AKRLGAVVMA TDVRAATKEQ VESLGGKFIT VDDEAMKTAE TAGGYAKEMG
     EEFRKKQAEA VLKELVKTDI AITTALIPGK PAPVLITEEM VTKMKPGSVI IDLAVEAGGN
     CPLSEPGKIV VKHGVKIVGH TNVPSRVAAD ASPLFAKNLL NFLTPHVDKD TKTLVMKLED
     ETVSGTCVTR DGAIVHPALT GQGA