ID Q8ZPL0_SALTY Unreviewed; 509 AA.
AC Q8ZPL0;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=NAD(P) transhydrogenase subunit alpha {ECO:0000256|PIRNR:PIRNR000203};
DE EC=7.1.1.1 {ECO:0000256|PIRNR:PIRNR000203};
GN Name=pntA {ECO:0000313|EMBL:AAL20398.1};
GN OrderedLocusNames=STM1479 {ECO:0000313|EMBL:AAL20398.1};
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287 {ECO:0000313|EMBL:AAL20398.1, ECO:0000313|Proteomes:UP000001014};
RN [1] {ECO:0000313|EMBL:AAL20398.1, ECO:0000313|Proteomes:UP000001014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720
RC {ECO:0000313|Proteomes:UP000001014};
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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:0000256|ARBA:ARBA00003943,
CC ECO:0000256|PIRNR:PIRNR000203}.
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:0000256|ARBA:ARBA00000006,
CC ECO:0000256|PIRNR:PIRNR000203};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005689, ECO:0000256|PIRNR:PIRNR000203}.
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DR EMBL; AE006468; AAL20398.1; -; Genomic_DNA.
DR RefSeq; NP_460439.1; NC_003197.2.
DR RefSeq; WP_001219362.1; NC_003197.2.
DR AlphaFoldDB; Q8ZPL0; -.
DR STRING; 99287.STM1479; -.
DR PaxDb; 99287-STM1479; -.
DR GeneID; 1252997; -.
DR KEGG; stm:STM1479; -.
DR PATRIC; fig|99287.12.peg.1562; -.
DR HOGENOM; CLU_003376_2_1_6; -.
DR OMA; YFPMLMT; -.
DR PhylomeDB; Q8ZPL0; -.
DR BioCyc; SENT99287:STM1479-MONOMER; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0006740; P:NADPH regeneration; IBA:GO_Central.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:InterPro.
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 InterPro; IPR026255; NADP_transhyd_a.
DR InterPro; IPR024605; NADP_transhyd_a_C.
DR NCBIfam; TIGR00561; pntA; 1.
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 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; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
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 Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR000203};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000203};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000203};
KW Oxidoreductase {ECO:0000313|EMBL:AAL20398.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001014};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|PIRNR:PIRNR000203};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 399..417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 423..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 454..471
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 477..498
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..137
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 146..311
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
FT REGION 376..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 509 AA; 54266 MW; ECCC3AB4537C0D2E CRC64;
MRIGIPKERL PNETRVAATP KTVEQLLKLG FSVAIESGAG QLASFDDKAF AQAGADIVDG
NAIWQSEIIL KVNAPEEEEI ALLNPGTTLV SFIWPAQNPG LMEKLAERKV TVMAMDSVPR
ISRAQSLDAL SSMANIAGYR AIVEAAHEFG RFFTGQITAA GKVPPAKVMV IGAGVAGLAA
IGAANSLGAI VRAFDTRPEV KEQVQSMGAE FLELDFKEEA GSGDGYAKVM SEAFIKAEMA
LFAAQAKEVD IIVTTALIPG KPAPKLITRD MVDSMKAGSV IVDLAAQNGG NCEYTVANQV
VTTDNGVKVI GYTDLPGRLP TQSSQLYGTN LVNLLKLLCK EKDGNIDVDF DDVVIRGVTV
IRDGDITWPA PPIQVSAQPQ AAPKAAPAPK EPEKPTSPWR KYALMALAII LFGWLADVAP
KEFLGHFTVF ALACVVGYYV VWNVSHALHT PLMSVTNAIS GIIVVGALLQ IGQGGWVSFL
SFIAVLIASI NIFGGFTVTQ RMLKMFRKN
//
