Q0H2X1 · Q0H2X1_9ACTN

  • Protein
    Putative aminotransferase
  • Gene
    atS13
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    2/5

Function

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

Features

Showing features for binding site, active site.

136950100150200250300350
TypeIDPosition(s)Description
Binding site54pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site55pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site161pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site182pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Active site187Proton acceptor
Binding site187pyridoxal 5'-phosphate (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
Molecular Functionpyridoxal phosphate binding
Molecular Functiontransaminase activity
Biological Processpolysaccharide biosynthetic process

Keywords

Names & Taxonomy

Protein names

  • Submitted names
    • Putative aminotransferase

Gene names

    • Name
      atS13

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • SCC 1655
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Streptosporangiales > Thermomonosporaceae > Actinomadura

Accessions

  • Primary accession
    Q0H2X1

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue187N6-(pyridoxal phosphate)lysine

Family & Domains

Sequence similarities

Belongs to the DegT/DnrJ/EryC1 family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    369
  • Mass (Da)
    41,007
  • Last updated
    2006-10-03 v1
  • Checksum
    9C6250D0A7E7DDD8
MIPLFKVAVSPTALDRVAEVFASGYLGQGPRVAEFESALAARLGNPRVVSVHSGTSGLCLALRLLDAPEERDEVLSTPLTFEATNWAILADGRRITWVDVDPATLTMDLDDLERKISPATRAIIVVHWTGYPVDLDRLAGILDRAEREHGFRPAVIEDCAHAWGASYRGVPLGSHGNMCVFSFQALKHLTCGDGGLLTLPGDELHERAMLRRFYGIDRTADRLRGAYDVAEWGLKWHMTDLNAAIGLANLETVDEQLRLHRENAAFYDKELTGVPGLELLQRSPDREGSFYVYDVKVDDRPAFHRKMEAAGIMAGLVSRRNDEHSCVAHLRTSLPGLDSVYDRMVSLPVGWWLTEQDREHVVATIRSGW

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DQ297453
EMBL· GenBank· DDBJ
ABC02793.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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