G9IIX7 · G9IIX7_PONPI

Function

function

Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.

Catalytic activity

Features

Showing features for binding site, site.

TypeIDPosition(s)Description
Binding site170-177ATP (UniProtKB | ChEBI)
Site363Required for activity

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentchloroplast thylakoid membrane
Cellular Componentproton-transporting ATP synthase complex, catalytic core F(1)
Molecular FunctionADP binding
Molecular FunctionATP binding
Molecular Functionproton-transporting ATP synthase activity, rotational mechanism
Molecular Functionproton-transporting ATPase activity, rotational mechanism

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    ATP synthase subunit alpha, chloroplastic
  • EC number
  • Alternative names
    • ATP synthase F1 sector subunit alpha
    • F-ATPase subunit alpha

Gene names

    • Name
      atpA
    • ORF names
      MipiCp026

Encoded on

  • Chloroplast

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > indigoferoid/millettioid clade > Millettieae > Pongamia

Accessions

  • Primary accession
    G9IIX7

Subcellular Location

Plastid membrane
; Peripheral membrane protein
Plastid, chloroplast thylakoid membrane
; Peripheral membrane protein

Keywords

Interaction

Subunit

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has four main subunits: a, b, b' and c.
F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain29-93ATPase F1/V1/A1 complex alpha/beta subunit N-terminal
Domain150-365ATPase F1/V1/A1 complex alpha/beta subunit nucleotide-binding
Domain372-496ATP synthase alpha subunit C-terminal

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    510
  • Mass (Da)
    55,709
  • Last updated
    2012-02-22 v1
  • Checksum
    F01A7400C5D57E11
MVTIRADEISKIIRERIEQYNTEVKIVNTGTVLQVGDGIARVYGLDEVMAGELVEFEEGTIGIALNLESKNVGVVLMGDGSMIQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIIVAETADSPATLQYLAPYTGAALAEYFMYRELHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSPQLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQSQSAPLTVEEQIITIYTGTNGYLDSLEIVRVKKFLVELRAYLKTNKPQFKEIISSTKTFTGEAEAILREAIQEEMELFLLQDQVEKN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JN673818
EMBL· GenBank· DDBJ
AET11349.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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