ID A0A3N2FFU9_9CELL Unreviewed; 508 AA.
AC A0A3N2FFU9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=EDF34_3164 {ECO:0000313|EMBL:ROS22989.1};
OS Cellulomonas sp. PhB150.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=2485188 {ECO:0000313|EMBL:ROS22989.1, ECO:0000313|Proteomes:UP000273256};
RN [1] {ECO:0000313|EMBL:ROS22989.1, ECO:0000313|Proteomes:UP000273256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PhB150 {ECO:0000313|EMBL:ROS22989.1,
RC ECO:0000313|Proteomes:UP000273256};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing
RT to study the core and pangenomes of soil and plant-associated
RT prokaryotes.";
RL Submitted (NOV-2018) 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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:ROS22989.1}.
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DR EMBL; RKHX01000005; ROS22989.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2FFU9; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000273256; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:1902600; P:proton transmembrane transport; 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 InterPro; IPR026255; NADP_transhyd_a.
DR InterPro; IPR024605; NADP_transhyd_a_C.
DR NCBIfam; TIGR00561; pntA; 1.
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 Pfam; PF12769; PNTB_4TM; 1.
DR PIRSF; PIRSF000203; NADP_transhydrogenase_alpha; 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 Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000273256};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 399..415
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 421..438
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 450..468
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 474..497
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..136
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 145..309
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 508 AA; 51934 MW; 3AFD1F147DDDBF38 CRC64;
MTTIGIPRET RPGERLVAAS PTSVGRLVGL GYDVVVEAGA GTAATYADEA YAEAGATIVE
NAWGADVVTA VNAPSDEQVA ALRAGAVLVA MLAPAAHPEL AERLRAQGVT ALALDAVPRI
SRAQSLDVLS TLSNVAGYRA VIEAAEQYGG MFGGQVTAAG KTAPARVFVI GAGVAGLAAI
GAADSLGAQV RAFDVRPEVA EQIESMGAAF VRAQSAQQQV STDGYASALT DEQEAATAAV
YAHESAEADV VITTALVRGT APTTITADMV AAMRPGSVIV DLAASGGGNC ELTVPGQRVV
TPNGVTIVGW TDLAGRLPRH TSQLFGTNVV HLLQLLTPGK DGVLVLDLED PVQRGMTVAH
GGDLLWPPPP VAVSAAPAPV PPPEPPAPAD PRPAARRRLV GFALAAVLVT LAISFAPPVF
LSHATVFVLA VFVGYYVISN VSHALHTPLM AQTNAISGII LVGALLQIGS DDWLVTTLAC
VAAALASINV FGGFLVANRM IRMFRRDA
//
