ID A0A257J1V8_9PROT Unreviewed; 377 AA.
AC A0A257J1V8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=CFE28_03045 {ECO:0000313|EMBL:OYU69061.1};
OS Alphaproteobacteria bacterium PA2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=2015570 {ECO:0000313|EMBL:OYU69061.1, ECO:0000313|Proteomes:UP000215921};
RN [1] {ECO:0000313|EMBL:OYU69061.1, ECO:0000313|Proteomes:UP000215921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA2 {ECO:0000313|EMBL:OYU69061.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
RL Submitted (JUN-2017) 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:OYU69061.1}.
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DR EMBL; NKIZ01000001; OYU69061.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257J1V8; -.
DR Proteomes; UP000215921; 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:UP000215921};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 5..140
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 149..316
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 377 AA; 38697 MW; FC9488D053DBE136 CRC64;
MTVIAVTKER RAGETRVAAT PETVKKLIAA GFSVTVEAGA GIAAAYPDAD YVAAGATLAK
TAKAAVEKAD ILYKVRAPED AEIAALKSGA IVAALLNPHQ DKAVVAALAA RGASAFAMEF
IPRITRAQVM DALSSQANLA GYRAVIEGAE AYGRALPMMM TAAGTIAAAK VFVMGVGVAG
LQAIATARRL GAVVTATDVR PATKEQVESL GAKFLAVEDE EFKNAQTAGG YAKEMSAEYQ
AKQAELVSSH IAKQDIVITT ALIPGRAAPR LVNAAQVASM RAGSVLVDLA VEQGGNVEGV
KPGEVLVTAN GVKILGIPNL PGRIATDASA LYARNLLAFS TLLLDKEGKL APDYEDEILK
AALVTQGGKV VHPALSA
//
