ID A0A0B6WU75_9BACT Unreviewed; 387 AA.
AC A0A0B6WU75;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=PYK22_00783 {ECO:0000313|EMBL:CDM64788.1};
OS Pyrinomonas methylaliphatogenes.
OC Bacteria; Acidobacteriota; Blastocatellia; Blastocatellales;
OC Pyrinomonadaceae; Pyrinomonas.
OX NCBI_TaxID=454194 {ECO:0000313|EMBL:CDM64788.1, ECO:0000313|Proteomes:UP000031518};
RN [1] {ECO:0000313|EMBL:CDM64788.1, ECO:0000313|Proteomes:UP000031518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K22 {ECO:0000313|EMBL:CDM64788.1,
RC ECO:0000313|Proteomes:UP000031518};
RA Stott M.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDM64788.1, ECO:0000313|Proteomes:UP000031518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K22 {ECO:0000313|EMBL:CDM64788.1,
RC ECO:0000313|Proteomes:UP000031518};
RA Lee K.C.Y., Power J.F., Dunfield P.F., Morgan X.C., Huttenhower C.,
RA Stott M.B.;
RT "Complete genome sequence of Pyrinomonas methylaliphatogenes type strain
RT K22T.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; CBXV010000003; CDM64788.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B6WU75; -.
DR STRING; 454194.PYK22_00783; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000031518; Unassembled WGS sequence.
DR GO; GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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; 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; PS00837; ALADH_PNT_2; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000313|EMBL:CDM64788.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031518};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 6..147
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 156..321
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 387 AA; 41354 MW; 177314950240CB76 CRC64;
MPITIGVVKE TFPEERRVAL TPNAVTQLKK AALEPLIENG AGAAAGFPDA AYAEAGATLL
PAREEIFRRA DIIVQVRALG ANPDRWSSDL ALMREGQTLI ALVEPLAAPD PVRAAAERGL
TTFALELIPR ITRAQTMDVL SSQANLAGYK AVIIAAQLLP KIFPMMMTAA GTITPARLFV
IGAGVAGLQA IATARRLGAV VSAYDVRPAV REQIESLGAR FVELPLEARD AQDASGYARA
MDEEFYRRQA ELLGDVIAEQ DVVISTAAVP GQRAPLLITR PMVERMAPGS VIVDLAAERG
GNCELTRPGE IIQHRGVYIS GPLNLPATLP FHASQLFARN VAAFILNLIR NGQIDPTADD
QIVAETLVTY AGQVVHQRVR QKLGLAA
//
