ID A4FLS7_SACEN Unreviewed; 366 AA.
AC A4FLS7;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN Name=pntAA {ECO:0000313|EMBL:CAM05002.1};
GN OrderedLocusNames=SACE_5818 {ECO:0000313|EMBL:CAM05002.1};
GN ORFNames=A8924_6160 {ECO:0000313|EMBL:PFG98639.1};
OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=405948 {ECO:0000313|EMBL:CAM05002.1, ECO:0000313|Proteomes:UP000006728};
RN [1] {ECO:0000313|EMBL:CAM05002.1, ECO:0000313|Proteomes:UP000006728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC {ECO:0000313|EMBL:CAM05002.1};
RX PubMed=17369815; DOI=10.1038/nbt1297;
RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA Haydock S.F., Leadlay P.F.;
RT "Complete genome sequence of the erythromycin-producing bacterium
RT Saccharopolyspora erythraea NRRL23338.";
RL Nat. Biotechnol. 25:447-453(2007).
RN [2] {ECO:0000313|EMBL:PFG98639.1, ECO:0000313|Proteomes:UP000225825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG98639.1,
RC ECO:0000313|Proteomes:UP000225825};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
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 ---------------------------------------------------------------------------
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; AM420293; CAM05002.1; -; Genomic_DNA.
DR EMBL; PDBV01000001; PFG98639.1; -; Genomic_DNA.
DR RefSeq; WP_009943178.1; NZ_PDBV01000001.1.
DR AlphaFoldDB; A4FLS7; -.
DR STRING; 405948.SACE_5818; -.
DR KEGG; sen:SACE_5818; -.
DR eggNOG; COG3288; Bacteria.
DR HOGENOM; CLU_003376_2_1_11; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000006728; Chromosome.
DR Proteomes; UP000225825; Unassembled WGS sequence.
DR GO; GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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 Oxidoreductase {ECO:0000313|EMBL:CAM05002.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006728};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 12..142
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 151..313
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 366 AA; 37579 MW; 679AD514CDB77B08 CRC64;
MTAQQSSRPS VGVPGESLVG ERRVALVPGV VERLRALGLD VVVEAGAGQR ALIPDEAFTE
AGASIGDAWS ADVVVKVNPP TAEEVGRLAA GTTLIGFLAP LTEPETTERL RAAGVTAFAM
ESIPRISRAQ SMDALSSQAN VAGYRAVLLA ASESTRFLPM LTTAAGTVKP ATALVLGVGV
AGLQALATAK RLGARTTGYD VRPEVADQVR SVGAKWLDLG IDATGEGGYA RALGADEAAE
QERRLGEAIA GFDIVVTTAL VPGKPAPRLV SADAVRAMRP GSVVVDLAGA TGGNCELSEP
GRTVVAHDVT IAAPLNLPAS MPEHASELYA RNVHALLELL VTDGRLAPDF GDEVLAASCV
TRQEEA
//
