ID A0A1W9JLF5_9PROT Unreviewed; 373 AA.
AC A0A1W9JLF5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=BVN33_12550 {ECO:0000313|EMBL:OQW72474.1};
OS Proteobacteria bacterium ST_bin13.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1978761 {ECO:0000313|EMBL:OQW72474.1, ECO:0000313|Proteomes:UP000192661};
RN [1] {ECO:0000313|EMBL:OQW72474.1, ECO:0000313|Proteomes:UP000192661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST_bin13 {ECO:0000313|EMBL:OQW72474.1};
RX PubMed=28390307; DOI=10.1016/j.watres.2017.03.042;
RA Wang Y., Ma L., Mao Y., Jiang X., Xia Y., Yu K., Li B., Zhang T.;
RT "Comammox in drinking water systems.";
RL Water Res. 116:332-341(2017).
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 -!- 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 -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005689}.
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:OQW72474.1}.
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DR EMBL; MSXQ01000018; OQW72474.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9JLF5; -.
DR Proteomes; UP000192661; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; 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 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 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 NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 4..138
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 147..313
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 373 AA; 37946 MW; 2CF97A4BEE4A42B9 CRC64;
MKIALLKEQA AGENRVAGTP ETVKKFIALG ATVSVEAGAG AGAAIADTQF ADAGAALGSR
AETLSGADIV LGVQGPDPAS LAGAAPGAWI VASLNPFGER ARVDSYAAAG FEALAMEFMP
RITRAQSMDI LSSQSNLSGY KAVLDAAAEY GRAFPMMMTA AGTVSAARVF VMGVGVAGLQ
AIATARRLGA QVSATDVRSA TKEQIQSLGA KPIFVENVKG IEGEGAGGYA GEMSPEYQAA
QAELVSSHIA KQDIVITTAL IPGRPAPRLI SDAQIATMRP GSVIVDLAVE AGGNVEGAVA
GEVVTVHGVK IVGHKNVAGR LAADSSALFA RNLFNFLSAF WDKESGKPVL DEEIGDAIRL
TKDGKVVNAG LLG
//
