Q2RSB2 · PNTAA_RHORT

Function

function

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

Catalytic activity

Features

Showing features for binding site.

138450100150200250300350
TypeIDPosition(s)Description
Binding site127-129NAD+ (UniProtKB | ChEBI)
Binding site132-135NAD+ (UniProtKB | ChEBI)
Binding site180-182NAD+ (UniProtKB | ChEBI)
Binding site202-204NAD+ (UniProtKB | ChEBI)
Binding site234NAD+ (UniProtKB | ChEBI)
Binding site247NAD+ (UniProtKB | ChEBI)
Binding site266NAD+ (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentplasma membrane
Molecular FunctionNAD binding
Molecular FunctionNAD(P)+ transhydrogenase (Si-specific) activity
Molecular FunctionNAD+ binding
Molecular FunctionNADH binding
Molecular FunctionNADP binding
Molecular Functionprotein dimerization activity
Molecular Functionproton-translocating NAD(P)+ transhydrogenase activity
Biological ProcessNADPH regeneration

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    NAD(P) transhydrogenase subunit alpha part 1
  • EC number
  • Alternative names
    • Nicotinamide nucleotide transhydrogenase subunit alpha 1
    • Proton-translocating transhydrogenase component 1
    • Pyridine nucleotide transhydrogenase subunit alpha 1
    • dI

Gene names

    • Name
      pntAA
    • Synonyms
      nntA1
    • Ordered locus names
      Rru_A2183

Organism names

Accessions

  • Primary accession
    Q2RSB2
  • Secondary accessions
    • Q60164

Proteomes

Subcellular Location

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis127No effect on interaction with PntB, but hydride transfer inhibited. Much weaker binding to NADH.
Mutagenesis132No 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.
Mutagenesis135No effect on interaction with PntB, but hydride transfer strongly inhibited. No effect on the binding affinity to NADH.
Mutagenesis138No effect on interaction with PntB, but hydride transfer strongly inhibited. No effect on the binding affinity to NADH.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002316631-384NAD(P) transhydrogenase subunit alpha part 1

Interaction

Subunit

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.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region126-136RQD loop; involved in interaction with PntB

Sequence similarities

Belongs to the AlaDH/PNT family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    384
  • Mass (Da)
    40,277
  • Last updated
    2006-01-24 v1
  • Checksum
    B886A640CE2BFA12
MKIAIPKERRPGEDRVAISPEVVKKLVGLGFEVIVEQGAGVGASITDDALTAAGATIASTAAQALSQADVVWKVQRPMTAEEGTDEVALIKEGAVLMCHLGALTNRPVVEALTKRKITAYAMELMPRISRAQSMDILSSQSNLAGYRAVIDGAYEFARAFPMMMTAAGTVPPARVLVFGVGVAGLQAIATAKRLGAVVMATDVRAATKEQVESLGGKFITVDDEAMKTAETAGGYAKEMGEEFRKKQAEAVLKELVKTDIAITTALIPGKPAPVLITEEMVTKMKPGSVIIDLAVEAGGNCPLSEPGKIVVKHGVKIVGHTNVPSRVAADASPLFAKNLLNFLTPHVDKDTKTLVMKLEDETVSGTCVTRDGAIVHPALTGQGA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U05294
EMBL· GenBank· DDBJ
AAA62493.1
EMBL· GenBank· DDBJ
Genomic DNA
CP000230
EMBL· GenBank· DDBJ
ABC22983.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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