ID Q30JP2_VIBCL Unreviewed; 412 AA.
AC Q30JP2;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
DE Flags: Fragment;
GN Name=pntA {ECO:0000313|EMBL:AAY87748.1};
OS Vibrio cholerae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=666 {ECO:0000313|EMBL:AAY87748.1};
RN [1] {ECO:0000313|EMBL:AAY87748.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=#75 {ECO:0000313|EMBL:AAY87762.1}, 2100
RC {ECO:0000313|EMBL:AAY87757.1}, 395 {ECO:0000313|EMBL:AAY87747.1}, 4808
RC {ECO:0000313|EMBL:AAY87760.1}, 66-2 {ECO:0000313|EMBL:AAY87761.1},
RC E506 {ECO:0000313|EMBL:AAY87759.1}, E9120
RC {ECO:0000313|EMBL:AAY87758.1}, M4287/77 {ECO:0000313|EMBL:AAY87749.1},
RC NCTC 5395 {ECO:0000313|EMBL:AAY87750.1}, NCTC 9420
RC {ECO:0000313|EMBL:AAY87756.1}, and SIMP/77
RC {ECO:0000313|EMBL:AAY87748.1};
RX PubMed=16318732;
RA Salim A., Lan R., Reeves P.R.;
RT "Vibrio cholerae pathogenic clones.";
RL Emerg. Infect. Dis. 11:1758-1760(2005).
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};
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DR EMBL; DQ021254; AAY87747.1; -; Genomic_DNA.
DR EMBL; DQ021255; AAY87748.1; -; Genomic_DNA.
DR EMBL; DQ021256; AAY87749.1; -; Genomic_DNA.
DR EMBL; DQ021257; AAY87750.1; -; Genomic_DNA.
DR EMBL; DQ021263; AAY87756.1; -; Genomic_DNA.
DR EMBL; DQ021264; AAY87757.1; -; Genomic_DNA.
DR EMBL; DQ021265; AAY87758.1; -; Genomic_DNA.
DR EMBL; DQ021266; AAY87759.1; -; Genomic_DNA.
DR EMBL; DQ021267; AAY87760.1; -; Genomic_DNA.
DR EMBL; DQ021268; AAY87761.1; -; Genomic_DNA.
DR EMBL; DQ021269; AAY87762.1; -; Genomic_DNA.
DR AlphaFoldDB; Q30JP2; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:InterPro.
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 InterPro; IPR026255; NADP_transhyd_a.
DR NCBIfam; TIGR00561; pntA; 1.
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 Membrane {ECO:0000256|SAM:Phobius}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 377..410
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..110
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 119..284
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
FT REGION 350..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAY87748.1"
FT NON_TER 412
FT /evidence="ECO:0000313|EMBL:AAY87748.1"
SQ SEQUENCE 412 AA; 43209 MW; 93CD24E60C2EC22C CRC64;
KLGFEVCIES KAGALASFDD AAYTAAGATI GSREEIWACP LILKVNAPSD DEIALLKEGA
TLVSFIWPAQ NPALMEKLSS KNINVLAMDA VPRISRAQAL DALSSMANIA GYRAVVEAAH
EFGRFFTGQI TAAGKVSPAK VFVAGAGVAG LAAIGAAGSL GAIVRAFDVR PEVKEQVQSM
GAEFLEVNFQ ETAGSGDGYA KEMSDEFNRK AAELYAAQAK DVDIIITTAL IPGKPAPKLI
TKEMVDSMKA GSVIVDLAAA NGGNCEYTVK DQVITTDNGV KVIGYTDMVG RLPTQSSQLY
ATNLVNLLKL LCKEKDGNID INFEDVVLRG VTVVKAGEIT WPAPPIQVSA QPQQKAKVQP
TKAQKKEPEP TSPVKKLVGL AVGVGLFAWV ASVAPAAFLG HFTVFVLACV VG
//
