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Database: UniProt
Entry: A0A1I6MPS5_9MICO
LinkDB: A0A1I6MPS5_9MICO
Original site: A0A1I6MPS5_9MICO 
ID   A0A1I6MPS5_9MICO        Unreviewed;       382 AA.
AC   A0A1I6MPS5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-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=SAMN04487846_3633 {ECO:0000313|EMBL:SFS17702.1};
OS   Microbacterium sp. cf046.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1761803 {ECO:0000313|EMBL:SFS17702.1, ECO:0000313|Proteomes:UP000199422};
RN   [1] {ECO:0000313|EMBL:SFS17702.1, ECO:0000313|Proteomes:UP000199422}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF046 {ECO:0000313|EMBL:SFS17702.1,
RC   ECO:0000313|Proteomes:UP000199422};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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};
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DR   EMBL; FOZJ01000003; SFS17702.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6MPS5; -.
DR   STRING; 1761803.SAMN04487846_3633; -.
DR   Proteomes; UP000199422; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
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   Reference proteome {ECO:0000313|Proteomes:UP000199422};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          6..139
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          148..315
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
SQ   SEQUENCE   382 AA;  38672 MW;  EB6708F7AC3E9230 CRC64;
     MTIHVRVRAE RSPGEKRVAA TPDSVKKLIA AGATVDIEAG AGAGSLITDA AYEAAGARIV
     QPDEPIEGGV LFHVRPLTAA EIATLPAGIV TIGTLDPFQN AAAVAAARDA GVTSFALDLL
     PRISRAQSMD VLSSQALLAG YRLVTLAADA FGRMFGMTMT AAGTLAPARV LVLGAGVAGL
     QAIATAKRLG GVVSANDVRA ASADEVRSVG GTFIDLDLGT AEAGGGYAKE LAEDRARRQQ
     ELLAPHIAAS DIVITTAAVP GRAAPRLVTT EMVAAMKPGS VLVDLAAESG GNIEGSVPGE
     RRAVVVTGGV VTLIGARDIQ SDLAPDASKL YAMNCVNFAA LIMKEGALVL DFDDELVSGS
     VVTHDGAVVN ERVAAAVEGV PA
//
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