ID A0A2N8S9U0_9GAMM Unreviewed; 373 AA. AC A0A2N8S9U0; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 22-FEB-2023, entry version 9. DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943}; DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943}; GN ORFNames=CXK98_19050 {ECO:0000313|EMBL:PNF99252.1}; OS Stutzerimonas kunmingensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Stutzerimonas. OX NCBI_TaxID=1211807 {ECO:0000313|EMBL:PNF99252.1, ECO:0000313|Proteomes:UP000236059}; RN [1] {ECO:0000313|EMBL:PNF99252.1, ECO:0000313|Proteomes:UP000236059} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCUG 36651 {ECO:0000313|EMBL:PNF99252.1, RC ECO:0000313|Proteomes:UP000236059}; RA Milligan D.A., Bergaust L., Bakken L.R., Frostegard A.; RT "Denitrification phenotypes of diverse strains of Pseudomonas stutzeri."; RL Submitted (JAN-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 -!- 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:PNF99252.1}. 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; POUV01000013; PNF99252.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2N8S9U0; -. DR EnsemblBacteria; PNF99252; PNF99252; CXK98_19050. DR Proteomes; UP000236059; Unassembled WGS sequence. 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; 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 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; PS00836; ALADH_PNT_1; 1. DR PROSITE; PS00837; ALADH_PNT_2; 1. PE 3: Inferred from homology; KW NAD {ECO:0000256|ARBA:ARBA00023027}. FT DOMAIN 4..136 FT /note="Alanine dehydrogenase/pyridine nucleotide FT transhydrogenase N-terminal" FT /evidence="ECO:0000259|SMART:SM01003" FT DOMAIN 145..314 FT /note="Alanine dehydrogenase/pyridine nucleotide FT transhydrogenase NAD(H)-binding" FT /evidence="ECO:0000259|SMART:SM01002" SQ SEQUENCE 373 AA; 38890 MW; 8015A9A6F7E7E460 CRC64; MHIGVPLETH SGETRVAATP ETVKKLIGQG HRVTLQSGAG LLSSVPDSAY EAVGATIGDA AAAFAAELVL KVNAPDDAEL AQMQSGSVLL GMLNPFDNAC IARMAARGVT AFALEAAPRT SRAQSLDVLS SQANIAGYKA VLVGAHHYPR FMPMLMTAAG TVKAARVLIL GAGVAGLQAI ATAKRLGAVV EASDVRPAVK EQIESLGAKF VDVPLETDEE RECAEGVGGY ARPMPASWMA RQAQAVHERA LQSDIVITTA LIPGRKAPTL LQEATVEQMK PGSVIVDLAA GHGGNCPLTE IDQVVVRHGV TIVGHANLAT LVAADASALY ARNLLDFLKL VIDKDGQFQL NLEDDIVAAC LMCRDGQVVR TNG //