ID A0A1H3SYI7_9PSEU Unreviewed; 365 AA.
AC A0A1H3SYI7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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=SAMN05421504_11658 {ECO:0000313|EMBL:SDZ42850.1};
OS Amycolatopsis xylanica.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=589385 {ECO:0000313|EMBL:SDZ42850.1, ECO:0000313|Proteomes:UP000199515};
RN [1] {ECO:0000313|EMBL:SDZ42850.1, ECO:0000313|Proteomes:UP000199515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CPCC 202699 {ECO:0000313|EMBL:SDZ42850.1,
RC ECO:0000313|Proteomes:UP000199515};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNON01000016; SDZ42850.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3SYI7; -.
DR STRING; 589385.SAMN05421504_11658; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000199515; 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:UP000199515};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 10..140
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 149..311
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 365 AA; 38029 MW; 0B44719F685DF8E0 CRC64;
MAETEQLTVG VVKESRSGER RVSLVPKLIE RLTKRGLRIV VESGAGEGAY LADSVFEEAG
AVIGDAWGAD IVLKVAPPTA DEVAKLKTGT LLIGFLNPRS DPDGITALEK AGVRAFAVEA
IPRISRAQAM DALSSQSGVA GYRAVLLAAE KLPRFFPMLT TAAGTVPPAK VLVLGAGVAG
LQALATAKRL GAQTTGYDVR PEVGEQVKSL GAKFLELGIE ASGEGGYARE LTEEERAEQQ
RRLTDAITKF DVVITTALVP GRKAPTLVTA EAVKGMPAGA VVVDLAGESG GNCELTKPGE
DVVEYDVTIT SPLNLPAEMP AHASELYARN VTELLELIVD KEGKLALDFS DEIVAGACVA
GKGAE
//
