ID A0A1G6IY58_9SPHN Unreviewed; 373 AA.
AC A0A1G6IY58;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=SAMN05444678_101387 {ECO:0000313|EMBL:SDC11492.1};
OS Sphingomonas sp. YR710.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1882773 {ECO:0000313|EMBL:SDC11492.1, ECO:0000313|Proteomes:UP000198912};
RN [1] {ECO:0000313|EMBL:SDC11492.1, ECO:0000313|Proteomes:UP000198912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR710 {ECO:0000313|EMBL:SDC11492.1,
RC ECO:0000313|Proteomes:UP000198912};
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};
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005689}.
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DR EMBL; FMZJ01000001; SDC11492.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6IY58; -.
DR STRING; 1882773.SAMN05444678_101387; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000198912; 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:UP000198912};
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; 38636 MW; 5EB009BBF41BEE32 CRC64;
MKIAVLKETA AGERRVSATP ETVKKFIALG AEVAVEAKAG VTASVADRAY SDVGATVGTR
EATLAGADII LGVQGPDPET LSGYHPGAWV VAGLNPFGER ARVDAYAAAG LEALAMEFMP
RITRAQSMDI LSSQSNLAGY KAVLDAASEY GRAFPMMMTA AGTISAARVF VMGVGVAGLQ
AIATARRLGA QVSATDVRSA TKEQIESLGA KAIFVENVKG IEGEGSGGYA TEMSDEYKAA
QAELVSSHIA KQDIVITTAL IPGRPAPRLI TDAQIATMKP GSVIVDLAVE AGGNVEGAVA
GKVANVRGVK IVGYTNVPSR LPADASALFS RNLYNFLSAF WDKEAGRPML DEEIGNAIRI
TQGGKVVNPR LLG
//
