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 27-MAR-2024, entry version 74.
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; Pseudomonadota; 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_DAMDTZ010000090.1.
DR AlphaFoldDB; P0C186; -.
DR SMR; P0C186; -.
DR TCDB; 3.D.2.2.1; the proton-translocating transhydrogenase (pth) family.
DR OMA; YFPMLMT; -.
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 CDD; cd05304; Rubrum_tdh; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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 PANTHER; PTHR10160; NAD(P) TRANSHYDROGENASE; 1.
DR PANTHER; PTHR10160:SF19; PROTON-TRANSLOCATING NAD(P)(+) TRANSHYDROGENASE; 1.
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; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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
//
