ID A0A0Q0ITP8_9GAMM Unreviewed; 395 AA.
AC A0A0Q0ITP8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN Name=pntAA {ECO:0000313|EMBL:KPZ69732.1};
GN ORFNames=AN944_02713 {ECO:0000313|EMBL:KPZ69732.1};
OS Shewanella sp. P1-14-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=1723761 {ECO:0000313|EMBL:KPZ69732.1, ECO:0000313|Proteomes:UP000050414};
RN [1] {ECO:0000313|EMBL:KPZ69732.1, ECO:0000313|Proteomes:UP000050414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1-14-1 {ECO:0000313|EMBL:KPZ69732.1,
RC ECO:0000313|Proteomes:UP000050414};
RA Gilbert D.G.;
RL Submitted (OCT-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}.
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:KPZ69732.1}.
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DR EMBL; LKTL01000017; KPZ69732.1; -; Genomic_DNA.
DR RefSeq; WP_055025128.1; NZ_LKTL01000017.1.
DR AlphaFoldDB; A0A0Q0ITP8; -.
DR PATRIC; fig|1723761.3.peg.2780; -.
DR Proteomes; UP000050414; 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:KPZ69732.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050414};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 4..142
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 151..316
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 395 AA; 41872 MW; 7AFDBAAAE40C0117 CRC64;
MKLGLPKESH SGEQRVALIP ANVTILMKKQ LQVIVESGAG LQAGFTDDDY VKVGATIASS
REALLTEADI ITVVNCKGDQ FDEISAVLKP HQLVIGMMDP LVNPQNAQTI ANTGGSAIAL
ELIPRITRAQ SMDVLSSMAT ISGYKAVLLA AHKAPRLFPM MMTAAGTLKP SRAFIMGVGV
AGLQACATAK RLGAVVEAYD IRPAAREQII SVGAKPVELD IEAENTETKG GYATEQSDDF
LKRQQQAMAN VLAQQDIVIT TAAIPGRKAP VLITKEMVDG MKSGTIIVDL AAESGGNCEL
TQVDEVIMHN GVMILGPSNV PSTAANHASQ MYGKNVENLL NLLINNEGEL VLDFEDEIVR
DTVVAHGNDV SSARLRELLN LAPLTAPESP SEETA
//
