ID A0A2N4WZ64_9SPHN Unreviewed; 376 AA.
AC A0A2N4WZ64;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, 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=C0V78_00730 {ECO:0000313|EMBL:PLK25581.1};
OS Novosphingobium sp. TH158.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=2067455 {ECO:0000313|EMBL:PLK25581.1, ECO:0000313|Proteomes:UP000234499};
RN [1] {ECO:0000313|EMBL:PLK25581.1, ECO:0000313|Proteomes:UP000234499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH158 {ECO:0000313|EMBL:PLK25581.1,
RC ECO:0000313|Proteomes:UP000234499};
RA Cai h.;
RT "genomes of bacteria within cyanobacterial aggregates.";
RL Submitted (DEC-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:PLK25581.1}.
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DR EMBL; PKRT01000001; PLK25581.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N4WZ64; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000234499; 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:UP000234499};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 8..140
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 149..315
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 376 AA; 38995 MW; C47FBFA4F72635F1 CRC64;
MAEALRIAVL KEHANGETRV AATPETVKKF IALGAAVAVE AGAGAGASIP DADYAAVGAE
VKSGAVTGAD IVLGVQGPEP KDLSGVRAGA WIVATLDPFR ERARVDEYAS LGLEALAMEF
MPRITRAQSM DVLSSQSNLA GYKAVIEAAN LYGRAFPMMM TAAGTVSAAK AFVMGVGVAG
LQAIATARRL GAQVSATDVR SATKEQIQSL GAKPIFVENV AGIEGEGAGG YATEMSEEYQ
KAQAELVSSH IAKQDIVITT ALIPGRPAPR LISDAQIASM KPGSVIFDLA VAQGGNVEGS
AADQVVEKHG VKILGYSNTP AKLPADASAL YARNLYNFLS AFWDKEQGKP VLDEEIGDAV
RLTRDGKVVN ERLLGA
//
