ID A0A117N322_RHILI Unreviewed; 426 AA.
AC A0A117N322;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=AU467_23420 {ECO:0000313|EMBL:KUM25955.1};
OS Rhizobium loti (Mesorhizobium loti).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=381 {ECO:0000313|EMBL:KUM25955.1, ECO:0000313|Proteomes:UP000053176};
RN [1] {ECO:0000313|EMBL:KUM25955.1, ECO:0000313|Proteomes:UP000053176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UFLA 01-765 {ECO:0000313|EMBL:KUM25955.1,
RC ECO:0000313|Proteomes:UP000053176};
RA Rangel W.M., Thijs S., Longatti S.M., Moreira F.M., Weyens N.,
RA Vangronsveld J., Van Hamme J.D., Bottos E.M., Rineau F.;
RT "Draft genome sequence of Mesorhizobium sp. UFLA 01-765, a multitolerant
RT efficient symbiont and plant-growth promoting strain isolated from Zn-
RT mining soil using Leucaena leucocephala as a trap plant.";
RL Submitted (DEC-2015) 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:KUM25955.1}.
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DR EMBL; LPWA01000110; KUM25955.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117N322; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000053176; Unassembled WGS sequence.
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 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..315
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
FT REGION 401..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 426 AA; 43978 MW; D7DCC06737B92F23 CRC64;
MGQTVFIPRE LDANEPRVAA SPETVKRLVG LGFEVIVEKG AGFGSRITDQ DFAAAGAAIG
KAADASKADV VLKVRRPTDA ELKGYKSGAA VIAIMDPYGN DAAVAAMAKA GITAFSMEFM
PRITRAQVMD VLSSQANLAG YQAVIDAAAE YDRALPMMMT AAGTVPAAKT FIMGVGVAGL
QAIATARRLG AVVTATDVRP AVKEQVQSLG AKFLAVEDEE FKAAETAGGY AKEMSKEYQA
KQAALTAEHI AKQDIVITTA LIPGRPAPKL VSAAMVASMK PGSVIVDLAV ERGGNVEGAV
AGKVVTTENG VKIVGHLNVP GRVAASASLL YAKNLYAFLE TMVDKAAKEL AIKRDDELVK
ATMLTDGGKV VHPNFAKAAE APRTEPAAIP ATIMVADTSD KPVAKKTAAK NPAAAKSPSS
KSKGTA
//