ID   PNTAA_RICPR             Reviewed;         383 AA.
AC   P41077;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 118.
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=Pyridine nucleotide transhydrogenase subunit alpha 1;
GN   Name=pntAA; OrderedLocusNames=RP863;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 215-383.
RC   STRAIN=Madrid E;
RX   PubMed=9335295; DOI=10.1128/jb.179.20.6448-6452.1997;
RA   Shaw E.I., Marks G.L., Winkler H.H., Wood D.O.;
RT   "Transcriptional characterization of the Rickettsia prowazekii major
RT   macromolecular synthesis operon.";
RL   J. Bacteriol. 179:6448-6452(1997).
RN   [3]
RP   GENE NAME.
RX   PubMed=8662004; DOI=10.1007/bf02352282;
RA   Andersson S.G.E., Sharp P.M.;
RT   "Codon usage and base composition in Rickettsia prowazekii.";
RL   J. Mol. Evol. 42:525-536(1996).
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       Rickettsia, the alpha chain is made of two subunits (PntAA and PntAB)
CC       and forms a dimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AlaDH/PNT family. {ECO:0000305}.
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DR   EMBL; AJ235273; CAA15287.1; -; Genomic_DNA.
DR   EMBL; U02878; AAB81400.1; -; Unassigned_DNA.
DR   PIR; G71648; G71648.
DR   RefSeq; NP_221211.1; NC_000963.1.
DR   RefSeq; WP_004596753.1; NC_000963.1.
DR   AlphaFoldDB; P41077; -.
DR   SMR; P41077; -.
DR   STRING; 272947.RP863; -.
DR   EnsemblBacteria; CAA15287; CAA15287; CAA15287.
DR   GeneID; 57569986; -.
DR   KEGG; rpr:RP863; -.
DR   PATRIC; fig|272947.5.peg.902; -.
DR   eggNOG; COG3288; Bacteria.
DR   HOGENOM; CLU_003376_2_1_5; -.
DR   OMA; YFPMLMT; -.
DR   Proteomes; UP000002480; Chromosome.
DR   GO; GO:0070403; F:NAD+ binding; ISS:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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.
PE   3: Inferred from homology;
KW   NAD; NADP; Nucleotide-binding; Reference proteome; Translocase.
FT   CHAIN           1..383
FT                   /note="NAD(P) transhydrogenase subunit alpha part 1"
FT                   /id="PRO_0000199020"
FT   BINDING         131..134
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         201..203
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         231
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   383 AA;  41638 MW;  70FC641B1F7C35C9 CRC64;
     MKIVALKEKV KNETRTAITP EVAGLLIKKG YAVTVEKDIG LYAGFLDEEY VAVGTKISSV
     PLEIISDADI ILKVQPSSVT DKYSELEFAK QGAIVVGLLS PYLNHEYIKA AAKKNLTTFA
     MEFVPRITKA QNMDALSSQS NLVGYRAVIE ASYHYTKAFP MMITAAGTIS ACKTLVLGVG
     VAGLQAIATA KRLGSIVAGY DVRIATKEQV ESLGAKFVSP ELQEDLEEES GYASESSADY
     KAKQEKFLAK IIKGYNIVIT TAQIPGKKAP MLVTDKMIES MMYGSVIVDI STSTGGNVEG
     SEPDKIVTRH GVTIIGLLNL ASKIASDSSK LYSKNLYNFL TYALQDGQFN MDDELVRDML
     ITKDGKIVNY IIREKYESIT DNG