ID U1F8E3_9ACTN Unreviewed; 515 AA.
AC U1F8E3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN Name=pntA {ECO:0000313|EMBL:ERF55733.1};
GN ORFNames=H641_07612 {ECO:0000313|EMBL:ERF55733.1}, L860_11670
GN {ECO:0000313|EMBL:OCT42203.1};
OS Cutibacterium granulosum DSM 20700.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Cutibacterium.
OX NCBI_TaxID=1160719 {ECO:0000313|EMBL:ERF55733.1, ECO:0000313|Proteomes:UP000016307};
RN [1] {ECO:0000313|EMBL:ERF55733.1, ECO:0000313|Proteomes:UP000016307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20700 {ECO:0000313|EMBL:ERF55733.1,
RC ECO:0000313|Proteomes:UP000016307};
RX PubMed=24053623; DOI=10.1186/1471-2164-14-640;
RA Mak T.N., Schmid M., Brzuszkiewicz E., Zeng G., Meyer R., Sfanos K.S.,
RA Brinkmann V., Meyer T.F., Bruggemann H.;
RT "Comparative genomics reveals distinct host-interacting traits of three
RT major human-associated propionibacteria.";
RL BMC Genomics 14:640-640(2013).
RN [2] {ECO:0000313|EMBL:OCT42203.1, ECO:0000313|Proteomes:UP000094467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20700 {ECO:0000313|EMBL:OCT42203.1,
RC ECO:0000313|Proteomes:UP000094467};
RA Jahns A.C., Eilers H., Alexeyev O.A.;
RL Submitted (MAY-2014) 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 -!- 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:ERF55733.1}.
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DR EMBL; AOSS01000285; ERF55733.1; -; Genomic_DNA.
DR EMBL; JNBU01000036; OCT42203.1; -; Genomic_DNA.
DR RefSeq; WP_021104525.1; NZ_AOSS01000285.1.
DR AlphaFoldDB; U1F8E3; -.
DR PATRIC; fig|1160719.4.peg.1429; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000016307; Unassembled WGS sequence.
DR Proteomes; UP000094467; 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; IPR008142; AlaDH/PNT_CS1.
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; PS00836; ALADH_PNT_1; 1.
PE 4: Predicted;
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 Oxidoreductase {ECO:0000313|EMBL:ERF55733.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016307};
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 405..425
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 431..450
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 482..504
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..137
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 146..315
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 515 AA; 54150 MW; 76840F0A4D35F33A CRC64;
MRIGIPREIV PGENRVAATP TTVAAIRKLG YDIAVEHHAG DNASLPDDAY EKAGATLTDS
TTVWGSDIVL AVNEPSDEQI GLMQRGAILV TFLHPRQDLE LTQKLQAAGI TGMSMDMVPR
ISRAQSMDAL SSMANISGYR AVVEAAHAYG RTFGGQVTAA GKVPPAKVFV IGTGVAGLAA
LGAANSMGAE VYATDVRPET AEQVQSMGAT FLHVRQSDAG GDQGVSSDGY AKETSDDYNA
RAAELYLEQA GKDDVIITTA AIPGKPSPKL ITADMVAAMK PGSVIVDLAA LGGGNCELTR
PGEKYVTDNG VTIIGYIDLP SRLAGQSSQL YGTNLVNLLK LVTPDKDGQI VLDMDDEVVR
TMTVCKDGEL LYPPPPVQVA AAPKPAAKAP EPVEEVKKEP RPWTYSFGIV TALAVVLIAL
LTFAPASFVE LFGTFAIAVV VGYYVVWNVT HALHTPLMSV TNAISGIIIV GAITQLGSGS
WAIKIIAAIT VLIASINIFG GFTVTQRMLK MFRKA
//
