ID A0A101AZB2_9MYCO Unreviewed; 374 AA.
AC A0A101AZB2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=AU194_06825 {ECO:0000313|EMBL:KUI31752.1};
OS Mycobacterium sp. GA-2829.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1772283 {ECO:0000313|EMBL:KUI31752.1, ECO:0000313|Proteomes:UP000053444};
RN [1] {ECO:0000313|EMBL:KUI31752.1, ECO:0000313|Proteomes:UP000053444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GA-2829 {ECO:0000313|EMBL:KUI31752.1,
RC ECO:0000313|Proteomes:UP000053444};
RG TB Trials Study Group;
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E.L., Macaden R.,
RA Grewal H.M.S.;
RL Submitted (JAN-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:KUI31752.1}.
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DR EMBL; LQIT01000026; KUI31752.1; -; Genomic_DNA.
DR RefSeq; WP_059090416.1; NZ_LQIT01000026.1.
DR AlphaFoldDB; A0A101AZB2; -.
DR STRING; 1772283.AU194_06825; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000053444; 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:UP000053444};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 9..139
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 148..310
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 374 AA; 38457 MW; F75B43C267F0F4D2 CRC64;
MERLATTVGV VGESAPDERR VALVPKAVAA LANAGVAVVV EPGAGERALL PDDLYVAAGA
SVGDAWAADV VVKVAPPSAE EAARLRRGQT LVGFLAPRSR DNQISTLAAA GVQAFAAEAV
PRISRAQAMD ALSSQANVAG YKAVLLAASE STRFFPMLTT AAGTVKPATV LVLGVGVAGL
QALATAKRLG ARTTGYDVRP EVADQVRSVG AQWLDLGIDA AGDGGYARDL SDDERRLQQK
RLEEAITGYD VVITTALVPG RPAPRLVTAA AVQGMKPGSV VVDLAGETGG NCELTDPGRT
VVRHDVTIAS PLNLPATMPE HASELYSKNI TALLGLLIKD GALQPDFADE IVAASCVTHA
SAAPSMPPTE ENHQ
//
