ID A0A1I5AX50_9GAMM Unreviewed; 378 AA.
AC A0A1I5AX50;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=SAMN05216289_1453 {ECO:0000313|EMBL:SFN66951.1};
OS Dokdonella immobilis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dokdonella.
OX NCBI_TaxID=578942 {ECO:0000313|EMBL:SFN66951.1, ECO:0000313|Proteomes:UP000198575};
RN [1] {ECO:0000313|EMBL:SFN66951.1, ECO:0000313|Proteomes:UP000198575}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7659 {ECO:0000313|EMBL:SFN66951.1,
RC ECO:0000313|Proteomes:UP000198575};
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};
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005689}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOVF01000045; SFN66951.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5AX50; -.
DR STRING; 578942.SAMN05216289_1453; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000198575; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000198575};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 6..139
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 148..311
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 378 AA; 39672 MW; D678A49468A8F9DF CRC64;
MPVVVAVLRE SAEGERRVAL TPEVAKKLKA RGAQIVMEKG AGASAYFPDA AFADAEVVAD
GPTALSRADV LLRVQPPTVE EIGHLREGTV VIAHLAPHLG PERVKALRDR KITAFAMELL
PRTTRAQAMD VLSSQAGVTG YKAVLIAAER APKFFPMLTT AAGTIRPSKV LIVGAGVAGL
QAIATARRLG AQVEGFDVRP ETREQIESLG AKFLDLGVSA AGSGGYAREL TAEEREQQQQ
ALANHLKNID VVVTTAAVPG RKAPRIISAA MIAGMKPGAV IVDIAAESGG NTELSKPGET
VVTDNGVSVI GTVNLPATTP INASEMYARN LYNFLELSLA DGALTLNWED ELIAKTCLTH
AGEIKHEPTK QAIEGASS
//
