ID A0A369ALR6_9BURK Unreviewed; 371 AA.
AC A0A369ALR6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=DFR45_10337 {ECO:0000313|EMBL:RCX10053.1};
OS Extensimonas vulgaris.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Extensimonas.
OX NCBI_TaxID=1031594 {ECO:0000313|EMBL:RCX10053.1, ECO:0000313|Proteomes:UP000252174};
RN [1] {ECO:0000313|EMBL:RCX10053.1, ECO:0000313|Proteomes:UP000252174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100911 {ECO:0000313|EMBL:RCX10053.1,
RC ECO:0000313|Proteomes:UP000252174};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-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 -!- 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:RCX10053.1}.
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DR EMBL; QPJU01000003; RCX10053.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369ALR6; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000252174; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000252174};
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 371 AA; 38332 MW; B9BA0F5953121CE8 CRC64;
MRIGVPAETM PGETRVAATP ETVKKLCAQG HQLCVQAGAG IAASVPDAAY QAAGAEIVDA
ATAFGADVVL KVRAPSAAEL ALLRPDAVLV GMLDPFDRAG LERLAQAGVS AFALEAAPRT
TRAQSMDVLS SQANVAGYKA VLLAANAYQR FFPMLMTAAG TVKAARVLVL GAGVAGLQAI
ATAKRLGAVI EASDVRPSVK EQVESLGAKF IDVPYETAEE KEAAEGVGGY ARPMPASWLE
RQKAEVAKRA ALADVLITTA LIPGRPAPVL VTEDMVRAMK PGSVIVDLAA HQGGNCPLTE
PGRTVLKHGV TLIGETNLPA LVAADASALY ARNVLDFLKL VLPKEGGVQI DLQEDIVAAC
LVAHQGAVTR K
//
