ID A0A246K4S4_9SPHN Unreviewed; 373 AA.
AC A0A246K4S4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=CDQ91_00855 {ECO:0000313|EMBL:OWR01009.1};
OS Sphingopyxis witflariensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=173675 {ECO:0000313|EMBL:OWR01009.1, ECO:0000313|Proteomes:UP000197097};
RN [1] {ECO:0000313|EMBL:OWR01009.1, ECO:0000313|Proteomes:UP000197097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14551 {ECO:0000313|EMBL:OWR01009.1,
RC ECO:0000313|Proteomes:UP000197097};
RX PubMed=12508864; DOI=10.1099/ijs.0.02217-0;
RA Kampfer P., Witzenberger R., Denner E.B., Busse H.J., Neef A.;
RT "Sphingopyxis witflariensis sp. nov., isolated from activated sludge.";
RL Int. J. Syst. Evol. Microbiol. 52:2029-2034(2002).
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 -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005689}.
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:OWR01009.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NISJ01000001; OWR01009.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A246K4S4; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000197097; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd05304; Rubrum_tdh; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR008143; Ala_DH/PNT_CS2.
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.
DR PROSITE; PS00837; ALADH_PNT_2; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000197097};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 4..138
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 147..313
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 373 AA; 38327 MW; 7812DAC01B3D4BBB CRC64;
MRIAVLKELA AGETRVAATP ETVKKFIGLG AEVAVEAGAG EQASVADADY SAAGAKVGSR
ADVLKGANII LAIQGPDPKG LKGFADGAWL AAGLNPFGER ARVDEYAKLG LEALAMEFMP
RITRAQSMDI LSSQANLAGY KAVLMAANAY GRAFPMMMTA AGTVSAAKAF VMGVGVAGLQ
AIATARRLGA QVSATDVRAA TKEQIMSLGA KPIFVETVAG IEGEGAGGYA TEMSDEYKAA
QAELVSSHIA KQDIVITTAL IPGRPAPRLI SDAQLATMRT GSVIVDMAAE SGGNVEGSVS
GEAKRIHGVT VIGASNIAAL MPADTSALFS RNLFNFLSAF WDKEAGKPVL DEEIGNAVRL
TQGGKVVSER LLG
//
