ID   PNTAB_RHORU             Reviewed;         139 AA.
AC   P0C187; Q59762; Q59764;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   28-JAN-2026, entry version 58.
DE   RecName: Full=NAD(P) transhydrogenase subunit alpha part 2;
DE            EC=7.1.1.1 {ECO:0000250|UniProtKB:Q2RSB2};
DE   AltName: Full=Nicotinamide nucleotide transhydrogenase subunit alpha 2;
DE   AltName: Full=Proton-translocating transhydrogenase component 2;
DE   AltName: Full=Pyridine nucleotide transhydrogenase subunit alpha 2;
DE   AltName: Full=dII;
GN   Name=pntAB; Synonyms=nntA2;
OS   Rhodospirillum rubrum.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rhodospirillales; 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=NAD(+) + NADPH + H(+)(in) = NADH + NADP(+) + H(+)(out);
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: Complex of an alpha and a beta chain; in Rhodospirillum, the
CC       alpha chain seems to be made of two subunits.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U01158; AAC43256.1; -; Genomic_DNA.
DR   RefSeq; WP_011390031.1; NZ_CP077803.1.
DR   AlphaFoldDB; P0C187; -.
DR   SMR; P0C187; -.
DR   TCDB; 3.D.2.2.1; the proton-translocating transhydrogenase (pth) family.
DR   OMA; LACVNIF; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050661; F:NADP binding; IEA:TreeGrafter.
DR   GO; GO:0008750; F:proton-translocating NAD(P)+ transhydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006740; P:NADPH regeneration; NAS:UniProtKB.
DR   InterPro; IPR024605; NADP_transhyd_a_C.
DR   PANTHER; PTHR10160; NAD(P) TRANSHYDROGENASE; 1.
DR   PANTHER; PTHR10160:SF19; PROTON-TRANSLOCATING NAD(P)(+) TRANSHYDROGENASE; 1.
DR   Pfam; PF12769; PNTB_4TM; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; NADP; Translocase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..139
FT                   /note="NAD(P) transhydrogenase subunit alpha part 2"
FT                   /id="PRO_0000199021"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   139 AA;  14889 MW;  04742D87817A8879 CRC64;
     MEDKNILVEG FNQLSQQALE LSQHAQALAL QASHAVLPAA AATEGASEFW WLMTVFVLAC
     FIGFYVVWSV TPALHSPLMG VTNAISSVIV VGALIATGPE AFSASKVLGF FAILLASVNI
     FGGFIVTQRM LAMFKKKQK
//