H5WYJ1 · H5WYJ1_9PSEU

Function

function

Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.

Catalytic activity

Cofactor

biotin (UniProtKB | Rhea| CHEBI:57586 )

Pathway

Carbohydrate biosynthesis; gluconeogenesis.

Features

Showing features for binding site, active site.

111271002003004005006007008009001,0001,100
Type
IDPosition(s)Description
Binding site117ATP (UniProtKB | ChEBI)
Binding site200ATP (UniProtKB | ChEBI)
Binding site238ATP (UniProtKB | ChEBI)
Active site295
Binding site536Mn2+ (UniProtKB | ChEBI)
Binding site608substrate
Binding site706Mn2+ (UniProtKB | ChEBI); via carbamate group
Binding site735Mn2+ (UniProtKB | ChEBI)
Binding site737Mn2+ (UniProtKB | ChEBI)
Binding site870substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionpyruvate carboxylase activity
Biological Processgluconeogenesis
Biological Processpyruvate metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Pyruvate carboxylase
  • EC number

Gene names

    • ORF names
      SacmaDRAFT_1303

Organism names

  • Taxonomic identifier
  • Strain
    • XMU15
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Pseudonocardiales > Pseudonocardiaceae > Saccharomonospora

Accessions

  • Primary accession
    H5WYJ1

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue706N6-carboxylysine
Modified residue1093N6-biotinyllysine

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain1-453Biotin carboxylation
Domain121-320ATP-grasp
Region479-509Disordered
Domain527-796Pyruvate carboxyltransferase
Region915-949Disordered
Compositional bias928-949Basic and acidic residues
Domain1053-1127Lipoyl-binding

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,127
  • Mass (Da)
    121,514
  • Last updated
    2012-04-18 v1
  • Checksum
    E24C17778B8824F1
MFRKVLVANRGEIAIRAFRAAYELGAGTVAVFPYEDRNSLHRLKADEAYEIGEQGHPVRAYLSVEEIVRAARMAGADAIYPGYGFLSENPELARACEEAGITFVGPSAEILQLTGNKARAVAAARQAGVPVLGSSAPSSDVDTLAAAAEELGFPVFVKAVAGGGGRGMRFVSNASTLRESIEAASREAESAFGDPTVFLEKAVVQPRHIEVQILADGTGGDDGVIHLYERDCSVQRRHQKVVELAPAPNLDPRLRDRICADAVRFARQIGYRNAGTVEFLVDRDGNHVFIEMNPRIQVEHTVTEEVTDVDLVQSQLRIAAGETLADLDLSQERIYLRGAALQCRITTEDPANGFRPDTGMISAYRSPGGSGIRLDGGTAFAGTEISAHFDSMLVKLTCRGRTFATAVGRARRAVAEFRIRGVATNIPFLQAVLDDPDFQAGRITTAFIEERPHLLTARHSADRGTRLLTYLADVTVNKPNGERPRLIDPERKLPTLPEGEPPPGSKQKLTELGPEGFARWLRESPHIGVTDTTFRDAHQSLLATRVRTKDLLAVAPVVAQTVPQLLSVECWGGATYDVALRFLAEDPWERLAALREAMPNLCLQMLLRGRNTVGYTPYPTEVTDAFVGEAAATGIDIFRIFDALNDVEQMRPAIDAVRATGTAVAEVALCYTSDLSNPAEKIYTLDYYLKLAEQIVGAGAHVLAIKDMAGLLRAPAAVKLVTALRREFDLPVHIHTHDTAGGQLGTYLAAIGAGADAVDGAVASMSGTTSQPSLSAIVAATDYSDRPTGLDLQAIGELEPYWEIVRKIYAPFEAGLASPTGRVYHHEIPGGQLSNLRSQARALGLGDRFEEIEAMYAAADRILGHLVKVTPSSKVVGDLALHLVGAGVSPEDFEAEPDKYDIPDSVIGFLRGELGDPPGGWPEPFRSKALRGRSEPRPVQPLSEEDRGELAADRRAALNRLLFPGPTKEFQVHRESYGDTSVLPSKDFFYGLRPGEEYAVDLEPGVRLLIELEAIGEADERGMRTVMATLNGQLRPIQVRDRSVASDLPAKEKADKNNPKHIAAPFAGVVTTSVAEGDTIEAGDTVATIEAMKMEAAITAPVGGTVQRLATNSVQQVEGGDLLLVLE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias928-949Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM001439
EMBL· GenBank· DDBJ
EHR49582.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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