ID A0A2H5EW86_9RHOB Unreviewed; 524 AA.
AC A0A2H5EW86;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=NAD(P) transhydrogenase subunit alpha {ECO:0000256|PIRNR:PIRNR000203};
DE EC=7.1.1.1 {ECO:0000256|PIRNR:PIRNR000203};
GN ORFNames=CX676_04635 {ECO:0000313|EMBL:AUH63540.1};
OS Paracoccus zhejiangensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1077935 {ECO:0000313|EMBL:AUH63540.1, ECO:0000313|Proteomes:UP000234530};
RN [1] {ECO:0000313|EMBL:AUH63540.1, ECO:0000313|Proteomes:UP000234530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J6 {ECO:0000313|EMBL:AUH63540.1,
RC ECO:0000313|Proteomes:UP000234530};
RX PubMed=23653121; DOI=10.1007/s10482-013-9932-2;
RA Wu Z.G., Zhang D.F., Liu Y.L., Wang F., Jiang X., Li C., Li S.P., Hong Q.,
RA Li W.J.;
RT "Paracoccus zhejiangensis sp. nov., isolated from activated sludge in
RT wastewater-treatment system.";
RL Antonie Van Leeuwenhoek 104:123-128(2013).
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; CP025430; AUH63540.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H5EW86; -.
DR KEGG; pzh:CX676_04635; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000234530; Chromosome.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000234530};
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 416..435
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 466..485
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 491..513
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..316
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 524 AA; 55401 MW; 49057C1DFF8851F1 CRC64;
MKIGALRETQ EGEARVAVTP SSAAHLQKLG HEVYVEAGAG KAAGFGDEDY RRAGVTVEAS
AADLIGAVDV VAKVRPPSEG EIGQMREGQT VISFFYPAQS AALLEQAKDQ GVTAIAMDMV
PRISRAQKMD ALSSMANIAG YRAVIEAANN FGRFFTGQVT AAGKVPPAKV LVVGAGVAGL
ASIGAAVSLG AQVYAFDVRP EVAEQIESMG AEFVYLDFSE AQTDGAATGG YAAPSSPEFR
EAQLARFREL APQMDIVITT ALIPGRDAPK LWTADMVAAM KTGSVIVDLA AERGGNCDLT
VPDERIVTEN GVVIIGYTDF PSRMGAQSSE LYGNNIRHFM ADLTPKKDGV IAHNMEDDVI
RGATVTHDHA ITYPPPPPKI AAIAAQKPKE KKKELTPEER RAAEAAAFKA ETRSQLMLLG
GGGLLLLLIG LVAPASFMSH FIVFVLACFV GFRVIWNVAH SLHTPLMAIT NAISSIIILG
ALMQIGSGSW LVLILAALSV LMAGVNIFGG FMVTRRMLAM FQKS
//
