ID A0A3M8G370_9BACT Unreviewed; 374 AA.
AC A0A3M8G370;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-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=ED557_05620 {ECO:0000313|EMBL:RNC84798.1};
OS Balneola sp.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Balneola.
OX NCBI_TaxID=2024824 {ECO:0000313|EMBL:RNC84798.1, ECO:0000313|Proteomes:UP000280416};
RN [1] {ECO:0000313|EMBL:RNC84798.1, ECO:0000313|Proteomes:UP000280416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bin6 {ECO:0000313|EMBL:RNC84798.1};
RA Zheng Q., Wang Y., Jiao N.;
RT "Metagenomics and metaproteomics analyze the interactions between
RT Synechococcus and associated heterotrophic bacteria in one oligotrophic
RT Synechococcus culture.";
RL Submitted (OCT-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:RNC84798.1}.
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DR EMBL; RHLJ01000002; RNC84798.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8G370; -.
DR Proteomes; UP000280416; 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; 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 Oxidoreductase {ECO:0000313|EMBL:RNC84798.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000280416};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 4..139
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 148..313
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 374 AA; 40278 MW; 1D2DAD4DBA816CE3 CRC64;
MIIAVLKETA EYERRVALTP DVVSQLVKKE LEVWVEKDAG VSANFPDAHY TEAGAKIVES
RSDILSDSDI ILAVQTPSTE DLKTIKSNTT LVCFLWALQH PDLVELLKSQ SISALGMDAI
PRISRAQNMD ALSSMSSIAG YKASLIAADT LDKYFPMMMT AAGTIPPSKA LILGAGVAGL
QAIATCRKLG AVVEAYDVRP VVKEQVESLG AKFVEIPLEE ENTETKGGYA KELSKDSQER
QKQVIHEHVK KSDIVITTAL IPGRPAPLLV TKEMVSDMKP GSVIVDLAAE NGGNCELTEA
GKTVNADGVN IVGPVNLPSQ LSNHASMLYA KNMLNLLNLL IKEGAADFNF EDEILLNTTI
THQGELISPS IKNN
//
