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Protein

NAD(P) transhydrogenase subunit alpha part 1

Gene

pntAA

Organism
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane.By similarity

Catalytic activityi

NADPH + NAD+ = NADP+ + NADH.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei234 – 2341NAD; via carbonyl oxygen3 Publications
Binding sitei247 – 2471NAD3 Publications
Binding sitei266 – 2661NAD; via carbonyl oxygen3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi127 – 1293NAD3 Publications
Nucleotide bindingi132 – 1354NAD3 Publications
Nucleotide bindingi180 – 1823NAD3 Publications
Nucleotide bindingi202 – 2043NAD3 Publications

GO - Molecular functioni

  • NAD(P)+ transhydrogenase (AB-specific) activity Source: UniProtKB
  • NAD(P)+ transhydrogenase (B-specific) activity Source: CACAO
  • NAD+ binding Source: UniProtKB
  • NAD binding Source: UniProtKB
  • NADH binding Source: UniProtKB
  • protein dimerization activity Source: UniProtKB

GO - Biological processi

  • hydrogen ion transmembrane transport Source: GOC
  • NADPH regeneration Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyciRRUB269796:GCN1-2218-MONOMER.
BRENDAi1.6.1.2. 5420.

Names & Taxonomyi

Protein namesi
Recommended name:
NAD(P) transhydrogenase subunit alpha part 1 (EC:1.6.1.2)
Alternative name(s):
Nicotinamide nucleotide transhydrogenase subunit alpha 1
Proton-translocating transhydrogenase component 1
Pyridine nucleotide transhydrogenase subunit alpha 1
dI
Gene namesi
Name:pntAA
Synonyms:nntA1
Ordered Locus Names:Rru_A2183
OrganismiRhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Taxonomic identifieri269796 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum
Proteomesi
  • UP000001929 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi127 – 1271R → A or M: No effect on interaction with PntB, but hydride transfer inhibited. Much weaker binding to NADH. 1 Publication
Mutagenesisi132 – 1321Q → N: No effect on interaction with PntB, but hydride transfer strongly inhibited. No effect on NADH binding affinity on its own, but differences in NADH binding properties in complex with PntB. 1 Publication
Mutagenesisi135 – 1351D → N: No effect on interaction with PntB, but hydride transfer strongly inhibited. No effect on the binding affinity to NADH. 1 Publication
Mutagenesisi138 – 1381S → A: No effect on interaction with PntB, but hydride transfer strongly inhibited. No effect on the binding affinity to NADH. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 384384NAD(P) transhydrogenase subunit alpha part 1PRO_0000231663Add
BLAST

Interactioni

Subunit structurei

Heterotrimer of two alpha chains and a beta (PntB) chain; in Rhodospirillum, the alpha chain is made of two subunits (PntAA and PntAB) and forms a dimer.5 Publications

GO - Molecular functioni

  • protein dimerization activity Source: UniProtKB

Protein-protein interaction databases

STRINGi269796.Rru_A2183.

Structurei

Secondary structure

1
384
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Beta strandi10 – 123Combined sources
Helixi20 – 289Combined sources
Beta strandi32 – 365Combined sources
Turni37 – 404Combined sources
Helixi41 – 433Combined sources
Helixi47 – 526Combined sources
Beta strandi56 – 605Combined sources
Helixi61 – 655Combined sources
Beta strandi69 – 757Combined sources
Helixi80 – 823Combined sources
Helixi86 – 894Combined sources
Beta strandi95 – 995Combined sources
Helixi102 – 1043Combined sources
Helixi106 – 1149Combined sources
Beta strandi118 – 1214Combined sources
Helixi122 – 1243Combined sources
Helixi129 – 1346Combined sources
Helixi136 – 15520Combined sources
Beta strandi163 – 1653Combined sources
Beta strandi168 – 1703Combined sources
Beta strandi174 – 1785Combined sources
Helixi182 – 19312Combined sources
Beta strandi197 – 2015Combined sources
Helixi208 – 2136Combined sources
Turni223 – 2286Combined sources
Beta strandi233 – 2353Combined sources
Helixi247 – 2559Combined sources
Beta strandi259 – 2635Combined sources
Beta strandi268 – 2703Combined sources
Helixi278 – 2814Combined sources
Beta strandi289 – 2924Combined sources
Helixi295 – 2973Combined sources
Beta strandi309 – 3124Combined sources
Beta strandi315 – 3184Combined sources
Helixi323 – 3275Combined sources
Helixi328 – 34316Combined sources
Helixi344 – 3463Combined sources
Turni349 – 3524Combined sources
Beta strandi358 – 3603Combined sources
Helixi361 – 3666Combined sources
Beta strandi367 – 3704Combined sources
Beta strandi371 – 3744Combined sources
Beta strandi379 – 3813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F8GX-ray2.00A/B/C/D1-384[»]
1HZZX-ray2.50A/B1-384[»]
1L7DX-ray1.81A/B/C/D1-384[»]
1L7EX-ray1.90A/B/C/D1-384[»]
1NM5X-ray2.40A/B1-384[»]
1PTJX-ray2.61A/B1-381[»]
1U28X-ray2.30A/B1-384[»]
1U2DX-ray3.00A/B1-384[»]
1U2GX-ray2.20A/B1-384[»]
1XLTX-ray3.10A/B/D/E/G/H1-384[»]
2FR8X-ray2.60A/B1-384[»]
2FRDX-ray3.20A/B1-384[»]
2FSVX-ray2.30A/B1-384[»]
2OO5X-ray2.60A/B1-384[»]
2OORX-ray2.32A/B1-384[»]
ProteinModelPortaliQ2RSB2.
SMRiQ2RSB2. Positions 1-380.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ2RSB2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni126 – 13611RQD loop; involved in interaction with PntBAdd
BLAST

Sequence similaritiesi

Belongs to the AlaDH/PNT family.Curated

Phylogenomic databases

eggNOGiENOG4108IIE. Bacteria.
COG3288. LUCA.
HOGENOMiHOG000022121.
KOiK00324.
OMAiVPKEIMH.
OrthoDBiEOG61P6S9.

Family and domain databases

InterProiIPR008143. Ala_DH/PNT_CS2.
IPR008142. AlaDH/PNT_CS1.
IPR007886. AlaDH/PNT_N.
IPR007698. AlaDH/PNT_NAD(H)-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01262. AlaDh_PNT_C. 1 hit.
PF05222. AlaDh_PNT_N. 1 hit.
[Graphical view]
SMARTiSM01002. AlaDh_PNT_C. 1 hit.
SM01003. AlaDh_PNT_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00836. ALADH_PNT_1. 1 hit.
PS00837. ALADH_PNT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2RSB2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIAIPKERR PGEDRVAISP EVVKKLVGLG FEVIVEQGAG VGASITDDAL
60 70 80 90 100
TAAGATIAST AAQALSQADV VWKVQRPMTA EEGTDEVALI KEGAVLMCHL
110 120 130 140 150
GALTNRPVVE ALTKRKITAY AMELMPRISR AQSMDILSSQ SNLAGYRAVI
160 170 180 190 200
DGAYEFARAF PMMMTAAGTV PPARVLVFGV GVAGLQAIAT AKRLGAVVMA
210 220 230 240 250
TDVRAATKEQ VESLGGKFIT VDDEAMKTAE TAGGYAKEMG EEFRKKQAEA
260 270 280 290 300
VLKELVKTDI AITTALIPGK PAPVLITEEM VTKMKPGSVI IDLAVEAGGN
310 320 330 340 350
CPLSEPGKIV VKHGVKIVGH TNVPSRVAAD ASPLFAKNLL NFLTPHVDKD
360 370 380
TKTLVMKLED ETVSGTCVTR DGAIVHPALT GQGA
Length:384
Mass (Da):40,277
Last modified:January 24, 2006 - v1
Checksum:iB886A640CE2BFA12
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U05294 Genomic DNA. Translation: AAA62493.1.
CP000230 Genomic DNA. Translation: ABC22983.1.
RefSeqiWP_011390032.1. NC_007643.1.
YP_427270.1. NC_007643.1.

Genome annotation databases

EnsemblBacteriaiABC22983; ABC22983; Rru_A2183.
GeneIDi3835610.
KEGGirru:Rru_A2183.
PATRICi23328064. VBIRhoRub82919_2277.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U05294 Genomic DNA. Translation: AAA62493.1.
CP000230 Genomic DNA. Translation: ABC22983.1.
RefSeqiWP_011390032.1. NC_007643.1.
YP_427270.1. NC_007643.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F8GX-ray2.00A/B/C/D1-384[»]
1HZZX-ray2.50A/B1-384[»]
1L7DX-ray1.81A/B/C/D1-384[»]
1L7EX-ray1.90A/B/C/D1-384[»]
1NM5X-ray2.40A/B1-384[»]
1PTJX-ray2.61A/B1-381[»]
1U28X-ray2.30A/B1-384[»]
1U2DX-ray3.00A/B1-384[»]
1U2GX-ray2.20A/B1-384[»]
1XLTX-ray3.10A/B/D/E/G/H1-384[»]
2FR8X-ray2.60A/B1-384[»]
2FRDX-ray3.20A/B1-384[»]
2FSVX-ray2.30A/B1-384[»]
2OO5X-ray2.60A/B1-384[»]
2OORX-ray2.32A/B1-384[»]
ProteinModelPortaliQ2RSB2.
SMRiQ2RSB2. Positions 1-380.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi269796.Rru_A2183.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABC22983; ABC22983; Rru_A2183.
GeneIDi3835610.
KEGGirru:Rru_A2183.
PATRICi23328064. VBIRhoRub82919_2277.

Phylogenomic databases

eggNOGiENOG4108IIE. Bacteria.
COG3288. LUCA.
HOGENOMiHOG000022121.
KOiK00324.
OMAiVPKEIMH.
OrthoDBiEOG61P6S9.

Enzyme and pathway databases

BioCyciRRUB269796:GCN1-2218-MONOMER.
BRENDAi1.6.1.2. 5420.

Miscellaneous databases

EvolutionaryTraceiQ2RSB2.
PROiQ2RSB2.

Family and domain databases

InterProiIPR008143. Ala_DH/PNT_CS2.
IPR008142. AlaDH/PNT_CS1.
IPR007886. AlaDH/PNT_N.
IPR007698. AlaDH/PNT_NAD(H)-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01262. AlaDh_PNT_C. 1 hit.
PF05222. AlaDh_PNT_N. 1 hit.
[Graphical view]
SMARTiSM01002. AlaDh_PNT_C. 1 hit.
SM01003. AlaDh_PNT_N. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00836. ALADH_PNT_1. 1 hit.
PS00837. ALADH_PNT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of the genes for the proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum and the implications for the domain structure of the enzyme."
    Williams R., Cotton N.P., Thomas C.M., Jackson J.B.
    Microbiology 140:1595-1604(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete sequence of the chromosome of Rhodospirillum rubrum ATCC 11170."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.
    , Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., Reslewic S., Zhou S., Schwartz D.C.
    Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1.
  3. "Protein-protein recognition, hydride transfer and proton pumping in the transhydrogenase complex."
    Buckley P.A., Jackson J.B., Schneider T., White S.A., Rice D.W., Baker P.J.
    Structure 8:809-815(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD.
    Strain: ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1.
  4. "The crystal structure of an asymmetric complex of the two nucleotide binding components of proton-translocating transhydrogenase."
    Cotton N.P.J., White S.A., Peake S.J., McSweeney S., Baz Jackson J.
    Structure 9:165-176(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD AND PNTB, SUBUNIT, REGION.
    Strain: ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1.
  5. "Crystal structures of transhydrogenase domain I with and without bound NADH."
    Prasad G.S., Wahlberg M., Sridhar V., Sundaresan V., Yamaguchi M., Hatefi Y., Stout C.D.
    Biochemistry 41:12745-12754(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF APO ENZYME, IN COMPLEX WITH NADH.
  6. "Glutamine 132 in the NAD(H)-binding component of proton-translocating transhydrogenase tethers the nucleotides before hydride transfer."
    van Boxel G.I., Quirk P.G., Cotton N.P., White S.A., Jackson J.B.
    Biochemistry 42:1217-1226(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF MUTANT ASN-132 IN COMPLEX WITH PNTB, CATALYTIC ACTIVITY, NADH-BINDING KINETICS, SUBSTRATE-NAD(P) TRANSHYDROGENASE PROTEIN COMPLEX KINETICS, SUBUNIT, MUTAGENESIS OF GLN-132.
    Strain: ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1.
  7. "Interactions between transhydrogenase and thio-nicotinamide Analogues of NAD(H) and NADP(H) underline the importance of nucleotide conformational changes in coupling to proton translocation."
    Singh A., Venning J.D., Quirk P.G., van Boxel G.I., Rodrigues D.J., White S.A., Jackson J.B.
    J. Biol. Chem. 278:33208-33216(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 1-381 IN COMPLEX WITH PNTB AND THIO-NICOTINAMIDE NUCLEOTIDE ANALOG, CATALYTIC ACTIVITY, SUBSTRATE ANALOG-NAD(P) TRANSHYDROGENASE PROTEIN COMPLEX KINETICS.
    Strain: ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1.
  8. "Active-site conformational changes associated with hydride transfer in proton-translocating transhydrogenase."
    Mather O.C., Singh A., van Boxel G.I., White S.A., Jackson J.B.
    Biochemistry 43:10952-10964(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEXES WITH NAD; NADH; ADP-RIBOSE AND PNTB.
    Strain: ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1.
  9. "Conformational diversity in NAD(H) and interacting transhydrogenase nicotinamide nucleotide binding domains."
    Sundaresan V., Chartron J., Yamaguchi M., Stout C.D.
    J. Mol. Biol. 346:617-629(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) IN COMPLEX WITH NAD AND PNTB.
  10. "The role of invariant amino acid residues at the hydride transfer site of proton-translocating transhydrogenase."
    Brondijk T.H., van Boxel G.I., Mather O.C., Quirk P.G., White S.A., Jackson J.B.
    J. Biol. Chem. 281:13345-13354(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF MUTANTS ALA-127; ASN-135 AND ALA-138 IN COMPLEXES WITH NAD; NADH AND PNTB, CATALYTIC ACTIVITY, SUBSTRATE-NAD(P) TRANSHYDROGENASE PROTEIN COMPLEX KINETICS, NADH-BINDING, MUTAGENESIS OF ARG-127; ASP-135 AND SER-138.
    Strain: ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1.
  11. "Structures of the dI2dIII1 complex of proton-translocating transhydrogenase with bound, inactive analogues of NADH and NADPH reveal active site geometries."
    Bhakta T., Whitehead S.J., Snaith J.S., Dafforn T.R., Wilkie J., Rajesh S., White S.A., Jackson J.B.
    Biochemistry 46:3304-3318(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) IN COMPLEXES WITH NAD; INACTIVE NADH ANALOG AND PNTB, CATALYTIC ACTIVITY, MOLECULAR DYNAMICS SIMULATIONS AND TRANSITION STATE MODELING OF NAD(P) TRANSHYDROGENASE PROTEIN COMPLEX.
    Strain: ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1.

Entry informationi

Entry nameiPNTAA_RHORT
AccessioniPrimary (citable) accession number: Q2RSB2
Secondary accession number(s): Q60164
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: January 24, 2006
Last modified: June 8, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.