ID A0A2W7RWW3_9BACT Unreviewed; 375 AA.
AC A0A2W7RWW3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 10.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=LX80_01005 {ECO:0000313|EMBL:PZX64804.1};
OS Hydrotalea sandarakina.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Hydrotalea.
OX NCBI_TaxID=1004304 {ECO:0000313|EMBL:PZX64804.1, ECO:0000313|Proteomes:UP000249720};
RN [1] {ECO:0000313|EMBL:PZX64804.1, ECO:0000313|Proteomes:UP000249720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23241 {ECO:0000313|EMBL:PZX64804.1,
RC ECO:0000313|Proteomes:UP000249720};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (JUN-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:PZX64804.1}.
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DR EMBL; QKZV01000002; PZX64804.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W7RWW3; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000249720; 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:UP000249720};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 4..137
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 146..311
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 375 AA; 40282 MW; A74D8F7AFF8952FB CRC64;
MIAGILKEPT GENRVSFLPE HLAGLLKLNI EIWVQENAGA AAYATNEVYQ QAGASIHSRS
EILQNAQIIF SILPLTNDDL QIIKPGTVVI GVYQPLYNYA EMQLWANKNL ITFSLDTIPR
TTRAQSMDVL SSQANIAGYK AVLLAAANYG RYFPMFITAA GSIPPAKVLV LGAGVAGLQA
IATAKRLGAV IEVFDTRPAV KEEVMSLGAK FVEVEGAADA SKAGGYAVEQ SAEYQQKQQQ
RIAEAAKKAD IIITTAQIPG KKAPLLLTEA MIQQMRNGSI IVDLAAATGG NTPLTKNNET
VVTENGVTIM GYSNLPGTMP FDASKLYGKN VFNFLQLIIS KEGKLNISFD DDIVKGCCIT
YNGKIVNERV LALNN
//
