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Database: UniProt
Entry: A0A432MDZ0_9BACT
LinkDB: A0A432MDZ0_9BACT
Original site: A0A432MDZ0_9BACT 
ID   A0A432MDZ0_9BACT        Unreviewed;       391 AA.
AC   A0A432MDZ0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, 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=TsocGM_22475 {ECO:0000313|EMBL:RUL83318.1};
OS   Tautonia sociabilis.
OC   Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC   Tautonia.
OX   NCBI_TaxID=2080755 {ECO:0000313|EMBL:RUL83318.1, ECO:0000313|Proteomes:UP000280296};
RN   [1] {ECO:0000313|EMBL:RUL83318.1, ECO:0000313|Proteomes:UP000280296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GM2012 {ECO:0000313|EMBL:RUL83318.1,
RC   ECO:0000313|Proteomes:UP000280296};
RA   Toschakov S.V.;
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RUL83318.1, ECO:0000313|Proteomes:UP000280296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GM2012 {ECO:0000313|EMBL:RUL83318.1,
RC   ECO:0000313|Proteomes:UP000280296};
RA   Kovaleva O.L., Elcheninov A.G., Van Heerden E., Toshchakov S.V.,
RA   Novikov A., Bonch-Osmolovskaya E.A., Kublanov I.V.;
RT   "Tautonia sociabilis, a novel thermotolerant planctomycete of
RT   Isosphaeraceae family, isolated from a 4000 m deep subterranean habitat.";
RL   Submitted (JAN-2019) 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:RUL83318.1}.
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DR   EMBL; RYZH01000062; RUL83318.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A432MDZ0; -.
DR   OrthoDB; 9804592at2; -.
DR   Proteomes; UP000280296; Unassembled WGS sequence.
DR   GO; GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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   Oxidoreductase {ECO:0000313|EMBL:RUL83318.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000280296};
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..319
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
SQ   SEQUENCE   391 AA;  41159 MW;  CE0DBB5C0A59F10D CRC64;
     MIIGIVRESF PGERRVALIP ASVPALTKAG FEVLVEPGAG APAGYPDESY QQKGASLAGS
     RDEVFSRADV LFHVLGFGAN PEAGRDDLPR YRPEQVVFGF LRPLGAPEAV AELARTGVTA
     FSIELLPRIT RAQRMDALSS MSTVAGYKAV LMAADALPRM FPMLMTAAGT ISPARVLVVG
     VGVAGLQAIA TAKRLGAVVS AYDIRPAVKE QVQSLGARFV ELPLETTQAE DVGGYARAQG
     EEFYRKQREL MARAVAESDV VITTANVPGR KAPVLITGEM VAGMNPGSVI VDMAAERGGN
     CALTRAGQTV SVHGVTILGA VNLASLVPFH ASQMYSSNLT TLLLHMARDG RLNIDTDDEI
     TRETLVARGG EVVHPRVLEA LGAAAGESRS S
//
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