ID A5GM90_SYNPW Unreviewed; 372 AA.
AC A5GM90;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN Name=pntAA {ECO:0000313|EMBL:CAK24055.1};
GN OrderedLocusNames=SynWH7803_1629 {ECO:0000313|EMBL:CAK24055.1};
OS Synechococcus sp. (strain WH7803).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=32051 {ECO:0000313|EMBL:CAK24055.1, ECO:0000313|Proteomes:UP000001566};
RN [1] {ECO:0000313|Proteomes:UP000001566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH7803 {ECO:0000313|Proteomes:UP000001566};
RG Genoscope;
RL Submitted (MAY-2006) 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}.
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DR EMBL; CT971583; CAK24055.1; -; Genomic_DNA.
DR AlphaFoldDB; A5GM90; -.
DR STRING; 32051.SynWH7803_1629; -.
DR KEGG; syx:SynWH7803_1629; -.
DR eggNOG; COG3288; Bacteria.
DR HOGENOM; CLU_003376_2_1_3; -.
DR OMA; YFPMLMT; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000001566; Chromosome.
DR GO; GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; IEA:UniProtKB-EC.
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:CAK24055.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001566};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 1..134
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 143..308
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 372 AA; 38959 MW; 7E27F497C56EBD06 CRC64;
METAVGETRV AASPETVKKF IALGCRVVLE RGAGQTSGFL DEAYAEAGAQ LVTPGDSQAW
GEADVLLCVQ SPSPVDLGRL RRGALVVGLL APYANIELDA ALKRCGLSAM ALELLPRISR
AQSADALSSQ ANIAGYKSVL LASAALDRYF PMLMTAAGTV QPARVVVLGA GVAGLQAVAT
ARRLGAVVYV SDIRPAVKEQ VESLGARFID PPEMEDKPAE SGGYAKQASD AFLAAQRQQL
SDQLSEADVA ICTAQVPGRR APRLISEDML DRMRPGAVVV DLAVAQGGNC ADTLPSQTVD
RKGVKLIGAN DLPCSVPNHA SFLYSKNLLA LLQPTLKDGQ LNLDLEDELI AGCLISQDGT
IRRSDVLTPG AN
//