ID   G3LH03_9PSED            Unreviewed;       373 AA.
AC   G3LH03;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE            EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
OS   Pseudomonas sp. 19-rlim.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1084570 {ECO:0000313|EMBL:AEO27397.1};
RN   [1] {ECO:0000313|EMBL:AEO27397.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=19-rlim {ECO:0000313|EMBL:AEO27397.1};
RA   Eaton R.W.;
RT   "Biodegradation of r-limonene and other terpenes by Pseudomonas sp. strain
RT   19-rlim.";
RL   Submitted (JUL-2011) 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};
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DR   EMBL; JN379032; AEO27397.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3LH03; -.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
DR   CDD; cd05304; Rubrum_tdh; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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.
PE   4: Predicted;
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..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;  38872 MW;  C30F7ADCEBBDD587 CRC64;
     MHIGVPLETH AGETRVAATP ETIKKLIGQG HQVTVQSGAG VSASIPDSAY EAVGATIGND
     AAAFAADLVL KVLAPTDAEL AHMRTGAVLV GMLNPFSNDT IARLNGRGIT AFALEAAPRT
     SRAQSLDVLS SQANIAGYKA VMLAANHYPR FMPMLMTAAG TVKAARVLIL GAGVAGLQAI
     ATAKRLGAVI EASDVRPAVK EQIESLGAKF VDVPFETDEE RECAQGVGGY ARPMPASWME
     RQAKAVHEKA KQADIVITTA LIPGRKAPTL LHEATVAEMK PGSVVIDLAA AQGGNCPLTE
     AEQVVVKHGV TIVGHSNLAA LVPADASALY ARNLLDFLKL VIDSEGKFHL NLEDDIVAAC
     LMCRDGQVVR TNG
//