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Database: UniProt
Entry: C0KDB7_VIBPH
LinkDB: C0KDB7_VIBPH
Original site: C0KDB7_VIBPH 
ID   C0KDB7_VIBPH            Unreviewed;       138 AA.
AC   C0KDB7;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 30.
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;
OS   Vibrio parahaemolyticus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=670 {ECO:0000313|EMBL:ACM90240.1};
RN   [1] {ECO:0000313|EMBL:ACM90240.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=K4250 {ECO:0000313|EMBL:ACM90240.1};
RX   PubMed=19749061; DOI=10.1128/AEM.01171-09;
RA   Hazen T.H., Martinez R.J., Chen Y., Lafon P.C., Garrett N.M., Parsons M.B.,
RA   Bopp C.A., Sullards M.C., Sobecky P.A.;
RT   "Rapid identification of Vibrio parahaemolyticus by whole-cell matrix-
RT   assisted laser desorption ionization-time of flight mass spectrometry.";
RL   Appl. Environ. Microbiol. 75:6745-6756(2009).
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; FJ577437; ACM90240.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0KDB7; -.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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   SMART; SM01002; AlaDh_PNT_C; 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   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          1..87
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACM90240.1"
FT   NON_TER         138
FT                   /evidence="ECO:0000313|EMBL:ACM90240.1"
SQ   SEQUENCE   138 AA;  15017 MW;  711F76850B946CF2 CRC64;
     GYAKEMSDDF NKKAAELYAE QAKDVDIFIT TALIPGRPAP KLITKEMVDS MKAGSVIVDL
     AAANGGNCEY TVKDQVIMTD NGVKIVGYTD MVGRLPTQSS QLYATNLVNL LKLLCKEKDG
     NINIDFEDVV LRGVTVIK
//
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