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Database: UniProt
Entry: A5GM90_SYNPW
LinkDB: A5GM90_SYNPW
Original site: A5GM90_SYNPW 
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
//
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