GenomeNet

Database: UniProt
Entry: G7G0R0_9GAMM
LinkDB: G7G0R0_9GAMM
Original site: G7G0R0_9GAMM 
ID   G7G0R0_9GAMM            Unreviewed;       512 AA.
AC   G7G0R0;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 33.
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:GAA78983.1};
GN   ORFNames=P20495_1478 {ECO:0000313|EMBL:GAA78983.1};
OS   Pseudoalteromonas sp. BSi20495.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=386429 {ECO:0000313|EMBL:GAA78983.1, ECO:0000313|Proteomes:UP000003050};
RN   [1] {ECO:0000313|Proteomes:UP000003050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSi20495 {ECO:0000313|Proteomes:UP000003050};
RX   PubMed=22275105; DOI=10.1128/JB.06427-11;
RA   Bian F., Xie B.B., Qin Q.L., Shu Y.L., Zhang X.Y., Yu Y., Chen B.,
RA   Chen X.L., Zhou B.C., Zhang Y.Z.;
RT   "Genome sequences of six Pseudoalteromonas strains isolated from Arctic sea
RT   ice.";
RL   J. Bacteriol. 194:908-909(2012).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAA78983.1}.
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; BADY01000048; GAA78983.1; -; Genomic_DNA.
DR   RefSeq; WP_008135221.1; NZ_BADY01000048.1.
DR   AlphaFoldDB; G7G0R0; -.
DR   Proteomes; UP000003050; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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; 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:GAA78983.1};
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        401..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        428..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        455..475
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        481..502
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          4..139
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          148..313
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
SQ   SEQUENCE   512 AA;  54099 MW;  6906852FD16EE14D CRC64;
     MKIGVPKEIR TGERRVATTP DAVSKLIKLG FNVAIETGAG MAANYTDDAY IAAGCEVVNS
     AQDIWAQSDI VLKVQAPEVD ENTLLKSGQT LICFLWPAQN PEILKDLTQR GITAIAIDSI
     PRISRAQKMD ARSSMANISG YRAIVEAAQH FGRFFTGQIT AAGRVAPAKV LVIGAGVAGL
     AAIGAAKSMG AIVRSFDTRA EVKEQIESMD AEFLMLDFKD EDGSGEGGYA KVMSDEFIEA
     EMALFAAQAK DVDIIVTTAL IPGKPAPKLI TSEMVASMNS GSVIVDLAAE QGGNCELTVP
     GKVAVCHGVS IIGYTDLPSR LATQSSQLYS NNLYNLLAEM TPEKDGELFV DMTNDVVLGA
     TICTEGKTTW PPPATTLSAT PKKVAATPIS TPTIVEKKKS VFGPIIGAAI GALALLGLGG
     VAPADFMSHF TVFVLACFVG YMVIWSVSPA LHTPLMSVTN AISSIIVIGA LIQISSTDDT
     IKWFAVFTVL IASINIVGGF AVTHRMLKMF RK
//
DBGET integrated database retrieval system