ID A0A2T0LWP8_9PSEU Unreviewed; 368 AA.
AC A0A2T0LWP8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=B0I33_104267 {ECO:0000313|EMBL:PRX48451.1};
OS Prauserella shujinwangii.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Prauserella.
OX NCBI_TaxID=1453103 {ECO:0000313|EMBL:PRX48451.1, ECO:0000313|Proteomes:UP000238362};
RN [1] {ECO:0000313|EMBL:PRX48451.1, ECO:0000313|Proteomes:UP000238362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7125 {ECO:0000313|EMBL:PRX48451.1,
RC ECO:0000313|Proteomes:UP000238362};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-2018) 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:PRX48451.1}.
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DR EMBL; PVNH01000004; PRX48451.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0LWP8; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000238362; 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:UP000238362};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 11..141
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 150..312
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 368 AA; 38549 MW; 774ACE670C0A4EEB CRC64;
MPETDSPPTI GVVKETKPGE RRVALVPKLV ERLVKRGLPV VVEKGAGAGA HLPDELYEQA
GASVGDAWSA DIVLRVAPPT RADIERLARG TILIGFLAPL SNVEEVAALE EAGVRAFAVE
SIPRISRAQS MDALSSQSSV AGYRATLLGA QRLTRFFPML TTAAGTVPPA KVLVLGAGVA
GLQALATAKR LGARATGYDV RPEVADQVRS VGAQWLDLGI EAVGEGGYAR ELTEEERAEQ
QRRLTEAITG FDVVITTALV PGRTAPTLVT ADAVRGMRPG SVVVDMAGEA GGNCELTEPG
KDVVVHDVTI CSPLNLPAEM PDHASELYAR NLVELVELLV DKEGNVNLDF SDEIIAGACV
AGAGEEVN
//
