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Database: UniProt
Entry: A0A1I5H1H7_9RHOB
LinkDB: A0A1I5H1H7_9RHOB
Original site: A0A1I5H1H7_9RHOB 
ID   A0A1I5H1H7_9RHOB        Unreviewed;       140 AA.
AC   A0A1I5H1H7;
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};
DE   Flags: Fragment;
GN   ORFNames=SAMN04487859_107175 {ECO:0000313|EMBL:SFN72033.1},
GN   SAMN04487859_1491 {ECO:0000313|EMBL:SFO42168.1};
OS   Roseovarius lutimaris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=1005928 {ECO:0000313|EMBL:SFO42168.1, ECO:0000313|Proteomes:UP000198599};
RN   [1] {ECO:0000313|EMBL:SFO42168.1, ECO:0000313|Proteomes:UP000198599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28463 {ECO:0000313|EMBL:SFO42168.1,
RC   ECO:0000313|Proteomes:UP000198599};
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; FOVP01000007; SFN72033.1; -; Genomic_DNA.
DR   EMBL; FOVP01000049; SFO42168.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5H1H7; -.
DR   STRING; 1005928.SAMN04487859_107175; -.
DR   Proteomes; UP000198599; Unassembled WGS sequence.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR007886; AlaDH/PNT_N.
DR   PANTHER; PTHR10160; NAD(P) TRANSHYDROGENASE; 1.
DR   PANTHER; PTHR10160:SF19; PROTON-TRANSLOCATING NAD(P)(+) TRANSHYDROGENASE; 1.
DR   Pfam; PF05222; AlaDh_PNT_N; 1.
DR   SMART; SM01003; AlaDh_PNT_N; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
PE   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          4..139
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   NON_TER         140
FT                   /evidence="ECO:0000313|EMBL:SFO42168.1"
SQ   SEQUENCE   140 AA;  14725 MW;  409704DD61D2303C CRC64;
     MKIGTPREVI EGENRVGMTP ESALQLQKLG HVCAIEAGAG VAAGFSDEAY AAAGVEIIKT
     AAALWKASDI VAKVRVPTDT EVKRLREGQT LISFFNPGGN EKQLKQAADK GATVVAMEMV
     PRISRAQKMD ALSSMANIAG
//
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