PNTA_CERSP
ID PNTA_CERSP Reviewed; 523 AA.
AC Q9ALA2;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=NAD(P) transhydrogenase subunit alpha {ECO:0000250|UniProtKB:P07001};
DE EC=7.1.1.1 {ECO:0000269|PubMed:11751816};
DE AltName: Full=Nicotinamide nucleotide transhydrogenase subunit alpha {ECO:0000250|UniProtKB:P07001};
DE AltName: Full=Pyridine nucleotide transhydrogenase subunit alpha {ECO:0000250|UniProtKB:P07001, ECO:0000312|EMBL:AAK00588.1};
GN Name=pntA {ECO:0000312|EMBL:AAK00588.1};
OS Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=1063;
RN [1] {ECO:0000312|EMBL:AAK00588.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=Ga {ECO:0000269|PubMed:11751816};
RX PubMed=11751816; DOI=10.1128/jb.184.2.400-409.2002;
RA Hickman J.W., Barber R.D., Skaar E.P., Donohue T.J.;
RT "Link between the membrane-bound pyridine nucleotide transhydrogenase and
RT glutathione-dependent processes in Rhodobacter sphaeroides.";
RL J. Bacteriol. 184:400-409(2002).
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:0000250|UniProtKB:P07001}.
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:0000269|PubMed:11751816};
CC -!- SUBUNIT: Heterodimer of an alpha (PntA) and a beta (PntB) chain.
CC {ECO:0000250|UniProtKB:P07001}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P07001}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P07001}.
CC -!- DISRUPTION PHENOTYPE: Loss of transhydrogenase activity. Sensitive to
CC aerobic methanol, but can utilize methanol as a sole carbon source in
CC the absence of oxygen. Not defective in formaldehyde oxidation under
CC anaerobic conditions. Increased specific activities of other NADPH-
CC producing enzymes. Has higher levels of glutathione disulfide and
CC increased sensitivity to oxidative stress agents like diamine in a
CC succinate-based minimal medium under aerobic conditions. However, the
CC size of the glutathione pool, levels of glutathione disulfide and
CC growth inhibition by diamide are comparable with wild-type when grown
CC aerobically in a glucose-based minimal medium indicating that glucose
CC utilization provides a means to the disruption mutants to maintain the
CC oxidation reduction state of glutathione pool and cytoplasmic proteins.
CC {ECO:0000269|PubMed:11751816}.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family. {ECO:0000255}.
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DR EMBL; AY026033; AAK00588.1; -; Genomic_DNA.
DR RefSeq; WP_002720404.1; NZ_CP051468.1.
DR AlphaFoldDB; Q9ALA2; -.
DR SMR; Q9ALA2; -.
DR OrthoDB; 464096at2; -.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
DR GO; GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; IDA:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0006116; P:NADH oxidation; IDA:UniProtKB.
DR GO; GO:0006740; P:NADPH regeneration; IDA:UniProtKB.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:InterPro.
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 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; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00561; pntA; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; NAD; NADP;
KW Nucleotide-binding; Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..523
FT /note="NAD(P) transhydrogenase subunit alpha"
FT /id="PRO_0000422045"
FT TOPO_DOM 1..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P07001, ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P07001, ECO:0000255"
FT TRANSMEM 433..455
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P07001, ECO:0000255"
FT TOPO_DOM 456..464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P07001, ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P07001, ECO:0000255"
FT TOPO_DOM 486..489
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P07001, ECO:0000255"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P07001, ECO:0000255"
FT TOPO_DOM 511..523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P07001, ECO:0000255"
FT BINDING 127..130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0C186"
FT BINDING 177
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P07001"
FT BINDING 197..199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P07001,
FT ECO:0000250|UniProtKB:P0C186"
FT BINDING 229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0C186"
SQ SEQUENCE 523 AA; 55619 MW; 45DFCF75683EF1C9 CRC64;
MKIGAPREIF EGEARVAMTP DSALQLQKLG HHCVIETGAG MKAGFSDEAY AAAGVEVLPS
AAALFEAADI VVKVRGPERA EAERLRRGQT LISFFWPAQN AELLELCKEK GATVVAMDMV
PRISRAQKMD ALSSMANIAG YRAVIEAGNN FGRFFTGQVT AAGKVPPAKV LVVGAGVAGL
AAIGTATSLG AITYAFDVRP EVAEQIESMG AEFVYLEFEE AQDGAATGGY AAPSSPEFRE
KQLAKFRELA PEMDIVITTA LIPGRPAPKL WTEDMVSAMK RGSVIVDLAS ERGGNCDLTV
PDQKIVTPNG VTIVGYTDFP SRMAAQASTL YSTNIRHMLT DLTPKKDGVI HHNMEDDVIR
GATVTHDGAI TFPPPPPKVA AIAAAKPREK VKELTPEEKR AAEIATFRKQ TVSQVAMLAV
GTALLLFVGM YAPPSFMAHF IVFALACFVG FQVIWNVSHS LHTPLMAVTN AISGIVILGA
LLQIGSGNVL VVLLAAISVL IATINIVGGF LVTRRMLAMF QKS
