PNTAA_RHORT
ID PNTAA_RHORT Reviewed; 384 AA.
AC Q2RSB2; Q60164;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=NAD(P) transhydrogenase subunit alpha part 1;
DE EC=7.1.1.1 {ECO:0000269|PubMed:12564924, ECO:0000269|PubMed:12791694, ECO:0000269|PubMed:16533815, ECO:0000269|PubMed:17323922};
DE AltName: Full=Nicotinamide nucleotide transhydrogenase subunit alpha 1;
DE AltName: Full=Proton-translocating transhydrogenase component 1;
DE AltName: Full=Pyridine nucleotide transhydrogenase subunit alpha 1;
DE AltName: Full=dI;
GN Name=pntAA; Synonyms=nntA1; OrderedLocusNames=Rru_A2183;
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8075801; DOI=10.1099/13500872-140-7-1595;
RA Williams R., Cotton N.P., Thomas C.M., Jackson J.B.;
RT "Cloning and sequencing of the genes for the proton-translocating
RT nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum and the
RT implications for the domain structure of the enzyme.";
RL Microbiology 140:1595-1604(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD.
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=10997900; DOI=10.1016/s0969-2126(00)00171-4;
RA Buckley P.A., Jackson J.B., Schneider T., White S.A., Rice D.W.,
RA Baker P.J.;
RT "Protein-protein recognition, hydride transfer and proton pumping in the
RT transhydrogenase complex.";
RL Structure 8:809-815(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD AND PNTB,
RP SUBUNIT, AND REGION.
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=11250201; DOI=10.1016/s0969-2126(01)00571-8;
RA Cotton N.P.J., White S.A., Peake S.J., McSweeney S., Baz Jackson J.;
RT "The crystal structure of an asymmetric complex of the two nucleotide
RT binding components of proton-translocating transhydrogenase.";
RL Structure 9:165-176(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF APO ENZYME, AND IN COMPLEX WITH
RP NADH.
RX PubMed=12379117; DOI=10.1021/bi020251f;
RA Prasad G.S., Wahlberg M., Sridhar V., Sundaresan V., Yamaguchi M.,
RA Hatefi Y., Stout C.D.;
RT "Crystal structures of transhydrogenase domain I with and without bound
RT NADH.";
RL Biochemistry 41:12745-12754(2002).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF MUTANT ASN-132 IN COMPLEX WITH
RP PNTB, CATALYTIC ACTIVITY, NADH-BINDING KINETICS, SUBSTRATE-NAD(P)
RP TRANSHYDROGENASE PROTEIN COMPLEX KINETICS, SUBUNIT, AND MUTAGENESIS OF
RP GLN-132.
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=12564924; DOI=10.1021/bi027032e;
RA van Boxel G.I., Quirk P.G., Cotton N.P., White S.A., Jackson J.B.;
RT "Glutamine 132 in the NAD(H)-binding component of proton-translocating
RT transhydrogenase tethers the nucleotides before hydride transfer.";
RL Biochemistry 42:1217-1226(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 1-381 IN COMPLEX WITH PNTB AND
RP THIO-NICOTINAMIDE NUCLEOTIDE ANALOG, CATALYTIC ACTIVITY, AND SUBSTRATE
RP ANALOG-NAD(P) TRANSHYDROGENASE PROTEIN COMPLEX KINETICS.
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=12791694; DOI=10.1074/jbc.m303061200;
RA Singh A., Venning J.D., Quirk P.G., van Boxel G.I., Rodrigues D.J.,
RA White S.A., Jackson J.B.;
RT "Interactions between transhydrogenase and thio-nicotinamide Analogues of
RT NAD(H) and NADP(H) underline the importance of nucleotide conformational
RT changes in coupling to proton translocation.";
RL J. Biol. Chem. 278:33208-33216(2003).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEXES WITH NAD; NADH;
RP ADP-RIBOSE AND PNTB.
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=15323555; DOI=10.1021/bi0497594;
RA Mather O.C., Singh A., van Boxel G.I., White S.A., Jackson J.B.;
RT "Active-site conformational changes associated with hydride transfer in
RT proton-translocating transhydrogenase.";
RL Biochemistry 43:10952-10964(2004).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) IN COMPLEX WITH NAD AND PNTB.
RX PubMed=15670609; DOI=10.1016/j.jmb.2004.11.070;
RA Sundaresan V., Chartron J., Yamaguchi M., Stout C.D.;
RT "Conformational diversity in NAD(H) and interacting transhydrogenase
RT nicotinamide nucleotide binding domains.";
RL J. Mol. Biol. 346:617-629(2005).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF MUTANTS ALA-127; ASN-135 AND
RP ALA-138 IN COMPLEXES WITH NAD; NADH AND PNTB, CATALYTIC ACTIVITY,
RP SUBSTRATE-NAD(P) TRANSHYDROGENASE PROTEIN COMPLEX KINETICS, NADH-BINDING,
RP AND MUTAGENESIS OF ARG-127; ASP-135 AND SER-138.
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=16533815; DOI=10.1074/jbc.m513230200;
RA Brondijk T.H., van Boxel G.I., Mather O.C., Quirk P.G., White S.A.,
RA Jackson J.B.;
RT "The role of invariant amino acid residues at the hydride transfer site of
RT proton-translocating transhydrogenase.";
RL J. Biol. Chem. 281:13345-13354(2006).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) IN COMPLEXES WITH NAD; INACTIVE NADH
RP ANALOG AND PNTB, CATALYTIC ACTIVITY, AND MOLECULAR DYNAMICS SIMULATIONS AND
RP TRANSITION STATE MODELING OF NAD(P) TRANSHYDROGENASE PROTEIN COMPLEX.
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=17323922; DOI=10.1021/bi061843r;
RA Bhakta T., Whitehead S.J., Snaith J.S., Dafforn T.R., Wilkie J., Rajesh S.,
RA White S.A., Jackson J.B.;
RT "Structures of the dI2dIII1 complex of proton-translocating
RT transhydrogenase with bound, inactive analogues of NADH and NADPH reveal
RT active site geometries.";
RL Biochemistry 46:3304-3318(2007).
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:12564924, ECO:0000269|PubMed:12791694,
CC ECO:0000269|PubMed:16533815, ECO:0000269|PubMed:17323922};
CC -!- SUBUNIT: Heterotrimer of two alpha chains and a beta (PntB) chain; in
CC Rhodospirillum, the alpha chain is made of two subunits (PntAA and
CC PntAB) and forms a dimer. {ECO:0000269|PubMed:10997900,
CC ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:12564924,
CC ECO:0000269|PubMed:12791694, ECO:0000269|PubMed:15670609}.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family. {ECO:0000305}.
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DR EMBL; U05294; AAA62493.1; -; Genomic_DNA.
DR EMBL; CP000230; ABC22983.1; -; Genomic_DNA.
DR RefSeq; WP_011390032.1; NC_007643.1.
DR RefSeq; YP_427270.1; NC_007643.1.
DR PDB; 1F8G; X-ray; 2.00 A; A/B/C/D=1-384.
DR PDB; 1HZZ; X-ray; 2.50 A; A/B=1-384.
DR PDB; 1L7D; X-ray; 1.81 A; A/B/C/D=1-384.
DR PDB; 1L7E; X-ray; 1.90 A; A/B/C/D=1-384.
DR PDB; 1NM5; X-ray; 2.40 A; A/B=1-384.
DR PDB; 1PTJ; X-ray; 2.61 A; A/B=1-381.
DR PDB; 1U28; X-ray; 2.30 A; A/B=1-384.
DR PDB; 1U2D; X-ray; 3.00 A; A/B=1-384.
DR PDB; 1U2G; X-ray; 2.20 A; A/B=1-384.
DR PDB; 1XLT; X-ray; 3.10 A; A/B/D/E/G/H=1-384.
DR PDB; 2FR8; X-ray; 2.60 A; A/B=1-384.
DR PDB; 2FRD; X-ray; 3.20 A; A/B=1-384.
DR PDB; 2FSV; X-ray; 2.30 A; A/B=1-384.
DR PDB; 2OO5; X-ray; 2.60 A; A/B=1-384.
DR PDB; 2OOR; X-ray; 2.32 A; A/B=1-384.
DR PDBsum; 1F8G; -.
DR PDBsum; 1HZZ; -.
DR PDBsum; 1L7D; -.
DR PDBsum; 1L7E; -.
DR PDBsum; 1NM5; -.
DR PDBsum; 1PTJ; -.
DR PDBsum; 1U28; -.
DR PDBsum; 1U2D; -.
DR PDBsum; 1U2G; -.
DR PDBsum; 1XLT; -.
DR PDBsum; 2FR8; -.
DR PDBsum; 2FRD; -.
DR PDBsum; 2FSV; -.
DR PDBsum; 2OO5; -.
DR PDBsum; 2OOR; -.
DR AlphaFoldDB; Q2RSB2; -.
DR SMR; Q2RSB2; -.
DR STRING; 269796.Rru_A2183; -.
DR EnsemblBacteria; ABC22983; ABC22983; Rru_A2183.
DR KEGG; rru:Rru_A2183; -.
DR PATRIC; fig|269796.9.peg.2277; -.
DR eggNOG; COG3288; Bacteria.
DR HOGENOM; CLU_003376_2_1_5; -.
DR OMA; YFPMLMT; -.
DR OrthoDB; 464096at2; -.
DR PhylomeDB; Q2RSB2; -.
DR BRENDA; 7.1.1.1; 5420.
DR EvolutionaryTrace; Q2RSB2; -.
DR PRO; PR:Q2RSB2; -.
DR Proteomes; UP000001929; Chromosome.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; IDA:UniProtKB.
DR GO; GO:0003957; F:NAD(P)+ transhydrogenase (B-specific) activity; IDA:CACAO.
DR GO; GO:0070403; F:NAD+ binding; IDA:UniProtKB.
DR GO; GO:0070404; F:NADH binding; IDA:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IDA:UniProtKB.
DR GO; GO:0006740; P:NADPH regeneration; IDA:UniProtKB.
DR InterPro; IPR008143; Ala_DH/PNT_CS2.
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 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; SSF51735; SSF51735; 1.
DR PROSITE; PS00836; ALADH_PNT_1; 1.
DR PROSITE; PS00837; ALADH_PNT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NAD; NADP; Nucleotide-binding; Reference proteome;
KW Translocase.
FT CHAIN 1..384
FT /note="NAD(P) transhydrogenase subunit alpha part 1"
FT /id="PRO_0000231663"
FT REGION 126..136
FT /note="RQD loop; involved in interaction with PntB"
FT BINDING 127..129
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10997900,
FT ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609"
FT BINDING 132..135
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10997900,
FT ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609"
FT BINDING 180..182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10997900,
FT ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609"
FT BINDING 202..204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10997900,
FT ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609"
FT BINDING 234
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10997900,
FT ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609"
FT BINDING 247
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10997900,
FT ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609"
FT BINDING 266
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10997900,
FT ECO:0000269|PubMed:11250201, ECO:0000269|PubMed:15670609"
FT MUTAGEN 127
FT /note="R->A,M: No effect on interaction with PntB, but
FT hydride transfer inhibited. Much weaker binding to NADH."
FT /evidence="ECO:0000269|PubMed:16533815"
FT MUTAGEN 132
FT /note="Q->N: No effect on interaction with PntB, but
FT hydride transfer strongly inhibited. No effect on NADH
FT binding affinity on its own, but differences in NADH
FT binding properties in complex with PntB."
FT /evidence="ECO:0000269|PubMed:12564924"
FT MUTAGEN 135
FT /note="D->N: No effect on interaction with PntB, but
FT hydride transfer strongly inhibited. No effect on the
FT binding affinity to NADH."
FT /evidence="ECO:0000269|PubMed:16533815"
FT MUTAGEN 138
FT /note="S->A: No effect on interaction with PntB, but
FT hydride transfer strongly inhibited. No effect on the
FT binding affinity to NADH."
FT /evidence="ECO:0000269|PubMed:16533815"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:1L7D"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:1PTJ"
FT HELIX 20..28
FT /evidence="ECO:0007829|PDB:1L7D"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:1L7D"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:1L7D"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1L7D"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:1L7D"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:1L7D"
FT HELIX 61..65
FT /evidence="ECO:0007829|PDB:1L7D"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:1L7D"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:1L7D"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:1L7D"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:1L7D"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1L7D"
FT HELIX 106..114
FT /evidence="ECO:0007829|PDB:1L7D"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:1L7D"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1L7D"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:1L7D"
FT HELIX 136..155
FT /evidence="ECO:0007829|PDB:1L7D"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:1L7D"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:1L7D"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:1L7D"
FT HELIX 182..193
FT /evidence="ECO:0007829|PDB:1L7D"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:1L7D"
FT HELIX 208..213
FT /evidence="ECO:0007829|PDB:1L7D"
FT TURN 223..228
FT /evidence="ECO:0007829|PDB:1U2G"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:1L7E"
FT HELIX 247..255
FT /evidence="ECO:0007829|PDB:1L7D"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:1L7D"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:1L7E"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:1L7D"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:1L7D"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:1L7D"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:1L7D"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:1L7D"
FT HELIX 323..327
FT /evidence="ECO:0007829|PDB:1L7D"
FT HELIX 328..343
FT /evidence="ECO:0007829|PDB:1L7D"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:1L7D"
FT TURN 349..352
FT /evidence="ECO:0007829|PDB:1L7D"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:1U28"
FT HELIX 361..366
FT /evidence="ECO:0007829|PDB:1L7D"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:1L7D"
FT STRAND 371..374
FT /evidence="ECO:0007829|PDB:2OO5"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:1L7D"
SQ SEQUENCE 384 AA; 40277 MW; B886A640CE2BFA12 CRC64;
MKIAIPKERR PGEDRVAISP EVVKKLVGLG FEVIVEQGAG VGASITDDAL TAAGATIAST
AAQALSQADV VWKVQRPMTA EEGTDEVALI KEGAVLMCHL GALTNRPVVE ALTKRKITAY
AMELMPRISR AQSMDILSSQ SNLAGYRAVI DGAYEFARAF PMMMTAAGTV PPARVLVFGV
GVAGLQAIAT AKRLGAVVMA TDVRAATKEQ VESLGGKFIT VDDEAMKTAE TAGGYAKEMG
EEFRKKQAEA VLKELVKTDI AITTALIPGK PAPVLITEEM VTKMKPGSVI IDLAVEAGGN
CPLSEPGKIV VKHGVKIVGH TNVPSRVAAD ASPLFAKNLL NFLTPHVDKD TKTLVMKLED
ETVSGTCVTR DGAIVHPALT GQGA
