ID H0F996_9BURK Unreviewed; 372 AA.
AC H0F996;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=KYC_16742 {ECO:0000313|EMBL:EHK65161.1};
OS Achromobacter arsenitoxydans SY8.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=477184 {ECO:0000313|EMBL:EHK65161.1, ECO:0000313|Proteomes:UP000003113};
RN [1] {ECO:0000313|EMBL:EHK65161.1, ECO:0000313|Proteomes:UP000003113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY8 {ECO:0000313|EMBL:EHK65161.1,
RC ECO:0000313|Proteomes:UP000003113};
RX PubMed=22328747; DOI=10.1128/JB.06667-11;
RA Li X., Hu Y., Gong J., Lin Y., Johnstone L., Rensing C., Wang G.;
RT "Genome sequence of the highly efficient arsenite-oxidizing bacterium
RT Achromobacter arsenitoxydans SY8.";
RL J. Bacteriol. 194:1243-1244(2012).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHK65161.1}.
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DR EMBL; AGUF01000055; EHK65161.1; -; Genomic_DNA.
DR RefSeq; WP_008164348.1; NZ_AGUF01000055.1.
DR AlphaFoldDB; H0F996; -.
DR STRING; 477184.KYC_16742; -.
DR PATRIC; fig|477184.5.peg.3303; -.
DR eggNOG; COG3288; Bacteria.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000003113; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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 Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 4..136
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 145..314
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 372 AA; 38669 MW; B9DF54C71F2E57BC CRC64;
MHIGIPKETR DGETRVAATP ETVKKYVGGK HTVVVERGAG SAARYLDEAY EAAGATLGSA
QDALGAELVM KVRAPSSHEL PHMKPGAAVV GMLDPFDAEG LAQMAAAGLV GFALEAAPRI
TRAQSLDVLS SQANLAGYKA VLLAAHHYGR LIPMMMTAAG TLKAARAVVL GTGVAGLQAI
ATAKRLGAVV EASDVRPAAR EQVESLGAKF IDVPFETDEE REIAQGTGGY ARPMPPAWMA
RQAALVSERC KQADIVITTA LIPGRPAPTL VSAETVAAMR PGSVLVDLAV ERGGNCPLSE
KGFIVEKHGV TLIGLTNLPG LVATDASALY ARNILDFLKL IINADGALAI QRDDEIVAAC
LVCEGGNVTR RT
//
