ID A0A2T5G044_9SPHN Unreviewed; 375 AA.
AC A0A2T5G044;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=CLG96_07245 {ECO:0000313|EMBL:PTQ12321.1};
OS Sphingomonas oleivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1735121 {ECO:0000313|EMBL:PTQ12321.1, ECO:0000313|Proteomes:UP000244162};
RN [1] {ECO:0000313|EMBL:PTQ12321.1, ECO:0000313|Proteomes:UP000244162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FW-11 {ECO:0000313|EMBL:PTQ12321.1,
RC ECO:0000313|Proteomes:UP000244162};
RA Wang L., Chen L.;
RT "Sphingomonas panjinensis sp.nov., isolated from oil-contaminated soil.";
RL Submitted (SEP-2017) 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};
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:PTQ12321.1}.
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DR EMBL; NWBU01000005; PTQ12321.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T5G044; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000244162; 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:UP000244162};
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 375 AA; 38804 MW; D92CD2901182B6BB CRC64;
MKIAVLREAA AGERRVAATP ETVKKLTALG AQLAVETGAG LTASISDKGY AEAGATVADR
AATLAGADII LGVQGPDPET LAGAKPGAWL VAALNPFGER ARVEAYAAAG LEALAMEFMP
RITRAQSMDI LSSQSNLAGY KAVLDAASEY GRAFPMMMTA AGTVSAARVF IMGVGVAGLQ
AIATARRLGA QVSATDVRSA TKEQILSLGA KPIFVEEVKG IEGEGSGGYA TEMSEEYKAK
QAELVSSHIA KQDIVITTAL IPGRPAPRLI SDAQLATMKP GSVIVDLAVE SGGNVEGAVA
GAIVERHGVK IVGHRNVPSR LAADASALFA RNLYNFLSAF WDKEAGRPVL PEDDEIGQAI
RLTQDGKVVN TRLLA
//
