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Database: UniProt
Entry: A0A0U0WEZ4_SALET
LinkDB: A0A0U0WEZ4_SALET
Original site: A0A0U0WEZ4_SALET 
ID   A0A0U0WEZ4_SALET        Unreviewed;       509 AA.
AC   A0A0U0WEZ4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 41.
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:SUE47567.1};
GN   ORFNames=B7N00_01465 {ECO:0000313|EMBL:EDG5015646.1}, B7N01_15785
GN   {ECO:0000313|EMBL:EDG4995886.1}, B7N35_05430
GN   {ECO:0000313|EMBL:EDG5125475.1}, B7N72_01465
GN   {ECO:0000313|EMBL:EDG5368796.1}, B7N78_15205
GN   {ECO:0000313|EMBL:EDG5281111.1}, B7N80_04845
GN   {ECO:0000313|EMBL:EDG5287717.1}, B7N84_10030
GN   {ECO:0000313|EMBL:EDG5266673.1}, DRU31_05745
GN   {ECO:0000313|EMBL:EBS2451833.1}, E0916_10885
GN   {ECO:0000313|EMBL:ECF1446456.1}, EJV93_11395
GN   {ECO:0000313|EMBL:ECA2721801.1}, EWC73_20265
GN   {ECO:0000313|EMBL:ECE8538510.1}, G0B02_06055
GN   {ECO:0000313|EMBL:HAC6378699.1}, G0D18_03675
GN   {ECO:0000313|EMBL:HAC6679785.1}, G2206_01520
GN   {ECO:0000313|EMBL:HAE0433476.1}, NCTC5754_02472
GN   {ECO:0000313|EMBL:SUE47567.1};
OS   Salmonella enterica subsp. enterica serovar Bovismorbificans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=58097 {ECO:0000313|EMBL:SUE47567.1, ECO:0000313|Proteomes:UP000254190};
RN   [1] {ECO:0000313|EMBL:HAC6378699.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6378699.1}, M123
RC   {ECO:0000313|EMBL:HAC6679785.1}, and MS140073
RC   {ECO:0000313|EMBL:HAE0433476.1};
RX   PubMed=30286803;
RA   Souvorov A., Agarwala R., Lipman D.J.;
RT   "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL   Genome Biol. 19:153-153(2018).
RN   [2] {ECO:0000313|EMBL:SUE47567.1, ECO:0000313|Proteomes:UP000254190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC5754 {ECO:0000313|EMBL:SUE47567.1,
RC   ECO:0000313|Proteomes:UP000254190};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:EBS2451833.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=136768 {ECO:0000313|EMBL:EDG4995886.1}, 138330
RC   {ECO:0000313|EMBL:EDG5287717.1}, 143652
RC   {ECO:0000313|EMBL:EDG5368796.1}, 273631
RC   {ECO:0000313|EMBL:EDG5015646.1}, 330535
RC   {ECO:0000313|EMBL:EDG5266673.1}, 333944
RC   {ECO:0000313|EMBL:EDG5281111.1}, 337042
RC   {ECO:0000313|EMBL:EDG5125475.1}, 387147
RC   {ECO:0000313|EMBL:EBS2451833.1}, 470200
RC   {ECO:0000313|EMBL:ECE8538510.1}, 598023
RC   {ECO:0000313|EMBL:ECA2721801.1}, and 692616
RC   {ECO:0000313|EMBL:ECF1446456.1};
RA   Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.;
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:HAC6378699.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6378699.1}, M123
RC   {ECO:0000313|EMBL:HAC6679785.1}, and MS140073
RC   {ECO:0000313|EMBL:HAE0433476.1};
RG   NCBI Pathogen Detection Project;
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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; AAGUWJ010000003; EBS2451833.1; -; Genomic_DNA.
DR   EMBL; AAHTVM010000005; ECA2721801.1; -; Genomic_DNA.
DR   EMBL; AAIJHK010000023; ECE8538510.1; -; Genomic_DNA.
DR   EMBL; AAIKGE010000005; ECF1446456.1; -; Genomic_DNA.
DR   EMBL; AAMEJW010000016; EDG4995886.1; -; Genomic_DNA.
DR   EMBL; AAMEJY010000001; EDG5015646.1; -; Genomic_DNA.
DR   EMBL; AAMEKY010000003; EDG5125475.1; -; Genomic_DNA.
DR   EMBL; AAMEMC010000004; EDG5266673.1; -; Genomic_DNA.
DR   EMBL; AAMEMH010000010; EDG5281111.1; -; Genomic_DNA.
DR   EMBL; AAMEML010000003; EDG5287717.1; -; Genomic_DNA.
DR   EMBL; AAMEMP010000001; EDG5368796.1; -; Genomic_DNA.
DR   EMBL; DAAMEZ010000003; HAC6378699.1; -; Genomic_DNA.
DR   EMBL; DAAMHM010000002; HAC6679785.1; -; Genomic_DNA.
DR   EMBL; DAAQQK010000001; HAE0433476.1; -; Genomic_DNA.
DR   EMBL; UGVQ01000002; SUE47567.1; -; Genomic_DNA.
DR   RefSeq; WP_001219360.1; NZ_WFIN01000001.1.
DR   AlphaFoldDB; A0A0U0WEZ4; -.
DR   Proteomes; UP000254190; Unassembled WGS sequence.
DR   Proteomes; UP000839929; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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:SUE47567.1};
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..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   509 AA;  54236 MW;  0CC39004537C0D34 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 EPEKPASPWR KYALMALAII LFGWLADVAP
     KEFLGHFTVF ALACVVGYYV VWNVSHALHT PLMSVTNAIS GIIVVGALLQ IGQGGWVSFL
     SFIAVLIASI NIFGGFTVTQ RMLKMFRKN
//
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