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RHORT:PNTAA

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Species (Taxon ID) Rhodospirillum rubrum (strain ATCC 11170 / NCIB 8255). (269796)
Gene Name(s) pntAA (synonyms: nntA1)
Protein Name(s) NAD(P) transhydrogenase subunit alpha part 1

Nicotinamide nucleotide transhydrogenase subunit alpha 1 Proton-translocating transhydrogenase component 1 Pyridine nucleotide transhydrogenase subunit alpha 1 dI

External Links
UniProt Q2RSB2
EMBL U05294
CP000230
RefSeq YP_427270.1
PDB 1F8G
1HZZ
1L7D
1L7E
1NM5
1PTJ
1U28
1U2D
1U2G
1XLT
2FR8
2FRD
2FSV
2OO5
2OOR
PDBsum 1F8G
1HZZ
1L7D
1L7E
1NM5
1PTJ
1U28
1U2D
1U2G
1XLT
2FR8
2FRD
2FSV
2OO5
2OOR
ProteinModelPortal Q2RSB2
SMR Q2RSB2
STRING 269796.Rru_A2183
EnsemblBacteria ABC22983
GeneID 3835610
KEGG rru:Rru_A2183
PATRIC 23328064
eggNOG COG3288
HOGENOM HOG000022121
KO K00324
OMA PNFEDEI
OrthoDB EOG61P6S9
BioCyc RRUB269796:GCN1-2218-MONOMER
EvolutionaryTrace Q2RSB2
Proteomes UP000001929
GO GO:0051287
GO:0008750
GO:0003957
GO:0070403
GO:0070404
GO:0046983
GO:1902600
GO:0006740
InterPro IPR008143
IPR008142
IPR007886
IPR007698
IPR026255
Pfam PF01262
PF05222
PIRSF PIRSF000203
SMART SM01002
SM01003
PROSITE PS00836
PS00837

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0008750

NAD(P)+ transhydrogenase (AB-specific) activity

PMID:8075801[1]

ECO:0000250

PMID:8232423[2]


F

Figure 3: Comparison of the domain and polypeptide structures of H+-Thase from R.rubrum, E.coli, bovine mitochondria and Ei.tenella and with alanine dehydrogenase from Bacillus stearothermophilus.

complete
CACAO 3299

GO:0003957

NAD(P)+ transhydrogenase (B-specific) activity

PMID:7556167[3]

ECO:0000314

F

Figure 5.0

complete
CACAO 3346

GO:0008750

NAD(P)+ transhydrogenase (AB-specific) activity

PMID:8075801[1]

ECO:0000314

F

Figure 6.

complete
CACAO 3451

enables

GO:0008750

NAD(P)+ transhydrogenase (AB-specific) activity

PMID:8075801[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003957

NAD(P)+ transhydrogenase (B-specific) activity

PMID:7556167[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0070404

NADH binding

PMID:16533815[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0070404

NADH binding

PMID:12564924[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0070404

NADH binding

PMID:12379117[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0070403

NAD+ binding

PMID:17323922[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0070403

NAD+ binding

PMID:15670609[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0070403

NAD+ binding

PMID:11250201[9]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0070403

NAD+ binding

PMID:10997900[10]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0051287

NAD binding

PMID:15323555[11]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0046983

protein dimerization activity

PMID:11250201[9]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008750

NAD(P)+ transhydrogenase (AB-specific) activity

PMID:17323922[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008750

NAD(P)+ transhydrogenase (AB-specific) activity

PMID:16533815[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008750

NAD(P)+ transhydrogenase (AB-specific) activity

PMID:12791694[12]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008750

NAD(P)+ transhydrogenase (AB-specific) activity

PMID:12564924[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006740

NADPH regeneration

PMID:17323922[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006740

NADPH regeneration

PMID:16533815[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006740

NADPH regeneration

PMID:12791694[12]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006740

NADPH regeneration

PMID:12564924[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:1902600

proton transmembrane transport

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0003957

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR008142
InterPro:IPR008143

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR008142
InterPro:IPR008143

P

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 1.2 Williams, R et al. (1994) 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. Microbiology (Reading, Engl.) 140 ( Pt 7) 1595-604 PubMed GONUTS page
  2. ↑ Kramer, RA et al. (1993) An Eimeria tenella gene encoding a protein with homology to the nucleotide transhydrogenases of Escherichia coli and bovine mitochondria. Mol. Biochem. Parasitol. 60 327-31 PubMed GONUTS page
  3. ↑ 3.0 3.1 Diggle, C et al. (1995) Conformational dynamics of a mobile loop in the NAD(H)-binding subunit of proton-translocating transhydrogenases from Rhodospirillum rubrum and Escherichia coli. Eur. J. Biochem. 232 315-26 PubMed GONUTS page
  4. ↑ 4.0 4.1 4.2 Brondijk, TH et al. (2006) The role of invariant amino acid residues at the hydride transfer site of proton-translocating transhydrogenase. J. Biol. Chem. 281 13345-54 PubMed GONUTS page
  5. ↑ 5.0 5.1 5.2 van Boxel, GI et al. (2003) Glutamine 132 in the NAD(H)-binding component of proton-translocating transhydrogenase tethers the nucleotides before hydride transfer. Biochemistry 42 1217-26 PubMed GONUTS page
  6. ↑ Prasad, GS et al. (2002) Crystal structures of transhydrogenase domain I with and without bound NADH. Biochemistry 41 12745-54 PubMed GONUTS page
  7. ↑ 7.0 7.1 7.2 Bhakta, T et al. (2007) Structures of the dI2dIII1 complex of proton-translocating transhydrogenase with bound, inactive analogues of NADH and NADPH reveal active site geometries. Biochemistry 46 3304-18 PubMed GONUTS page
  8. ↑ Sundaresan, V et al. (2005) Conformational diversity in NAD(H) and interacting transhydrogenase nicotinamide nucleotide binding domains. J. Mol. Biol. 346 617-29 PubMed GONUTS page
  9. ↑ 9.0 9.1 Cotton, NP et al. (2001) The crystal structure of an asymmetric complex of the two nucleotide binding components of proton-translocating transhydrogenase. Structure 9 165-76 PubMed GONUTS page
  10. ↑ Buckley, PA et al. (2000) Protein-protein recognition, hydride transfer and proton pumping in the transhydrogenase complex. Structure 8 809-15 PubMed GONUTS page
  11. ↑ Mather, OC et al. (2004) Active-site conformational changes associated with hydride transfer in proton-translocating transhydrogenase. Biochemistry 43 10952-64 PubMed GONUTS page
  12. ↑ 12.0 12.1 Singh, A et al. (2003) 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. J. Biol. Chem. 278 33208-16 PubMed GONUTS page
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