ID A0A1S8D7F4_9PROT Unreviewed; 384 AA.
AC A0A1S8D7F4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=APZ41_007250 {ECO:0000313|EMBL:ONH83859.1};
OS Roseomonas mucosa.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Roseomonas.
OX NCBI_TaxID=207340 {ECO:0000313|EMBL:ONH83859.1, ECO:0000313|Proteomes:UP000054844};
RN [1] {ECO:0000313|EMBL:ONH83859.1, ECO:0000313|Proteomes:UP000054844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAVE376 {ECO:0000313|EMBL:ONH83859.1,
RC ECO:0000313|Proteomes:UP000054844};
RA Choudhury M.A., Sidjabat H.E., Wailan A.M., Zhang L., Marsh N.M.,
RA Rickard C.M., Davies M., Mcmillan D.J.;
RT "Draft genome sequence of Roseomonas mucosa strain AU37, isolated from a
RT peripheral intravenous catheter.";
RL Submitted (DEC-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 -!- 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:ONH83859.1}.
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DR EMBL; LLWF02000016; ONH83859.1; -; Genomic_DNA.
DR RefSeq; WP_058390629.1; NZ_LLWF02000016.1.
DR AlphaFoldDB; A0A1S8D7F4; -.
DR STRING; 207340.APZ41_007250; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000054844; 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:UP000054844};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 4..145
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 154..321
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 384 AA; 39175 MW; 10F5BFA62AB84516 CRC64;
MRLAVPKERR ATEARVAATP ETVRKLIGLG LSVAVEKGAG LAAGIPDAAY AEAGAEIAPD
AAAALAGAGI VLKVRAPLAA GEGEVDEIAL IPEGAVLIGT LEAASAPERN RAYAARRITA
CAMELAPRIT RAQSMDVLSS QANLAGYRAV IEAAGAFDRG FPMLMTAAGT IPAANVLVLG
AGVAGLQAIA TARRLGGRVS ASDVRPAAKE EIKSLGASFV GVEDEESAAA QTAGGYAKAM
SPEYLRKQAE VVAAAAARAD IVICTALVQG RKAPVLLTEA MVAAMKPGAV VVDIAADAGG
NCAATVPGEA VTTENGVKVL GWRNWPARIP AAASSLYARN LLTFLTTFWD KEAGMPKLPE
EDEIVRGVLL TRGGAVVHPQ FQNS
//
