A0A5F1S1I3 · A0A5F1S1I3_9HYPH

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

biotin (UniProtKB | Rhea| CHEBI:57586 )

Pathway

Carbohydrate biosynthesis; gluconeogenesis.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site124ATP (UniProtKB | ChEBI)
Binding site208ATP (UniProtKB | ChEBI)
Active site301
Binding site548Mn2+ (UniProtKB | ChEBI)
Binding site620substrate
Binding site717Mn2+ (UniProtKB | ChEBI); via carbamate group
Binding site746Mn2+ (UniProtKB | ChEBI)
Binding site748Mn2+ (UniProtKB | ChEBI)
Binding site881substrate

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

    • Name
      pyc
    • ORF names
      C9417_21235

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • SEMIA 4088
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Rhizobiaceae > Rhizobium/Agrobacterium group > Rhizobium

Accessions

  • Primary accession
    A0A5F1S1I3

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue717N6-carboxylysine
Modified residue1118N6-biotinyllysine

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-462Biotin carboxylation
Domain128-326ATP-grasp
Domain539-807Pyruvate carboxyltransferase
Domain1077-1152Lipoyl-binding

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,153
  • Mass (Da)
    126,422
  • Last updated
    2019-11-13 v1
  • MD5 Checksum
    FF3DBE8F80502FC370866D7965C5F51E
MPISKILVANRSEIAIRVFRAANELGIKTVAIWAEEDKLALHRFKADESYQVGRGPHLARDLGPIESYLSIEEVIRVAKLSGADAIHPGYGLLSESPEFVDACDAAGIIFIGPRADTMRQLGNKVAARNLAISVGVPVVPATDPLPDDMAEVAKMAAEIGYPVMLKASWGGGGRGMRVIRSEADLAKEVTEAKREAKAAFGKDEVYLEKLVERARHVESQILGDTHGNVVHLFERDCSVQRRNQKVVERAPAPYLTEAQRQELAAYSLKIANATNYVGAGTVEYLMDADTGKFYFIEVNPRIQVEHTVTEVVTGIDIVKAQIHILDGFAIGTPESGVPKQEDIRLNGHALQCRVTTEDPEHNFIPDYGRITAYRSASGFGIRLDGGTSYTGAIITRYYDPLLVKVTAWAPNPQEAIARMYRALREFRIRGVATNLTFLEAIITHEKFRDNSYTTRFIDTTPELFQQVKRQDRATKLLTYLADVTVNGHPETRGRPVPSPKVAQPVLPYIDGNIPEGTKQLLDKLGPQKFAEWMRNEKRVLMTDTTMRDGHQSLLATRMRTYDIASVAGTYARALPQLLSLECWGGATFDVSMRFLTEDPWERLALIREGAPNLLLQMLLRGANGVGYTNYPDNVVKYFVRQAAKGGVDLFRVFDCLNWVENMRVSMDAVAEENKLCEAAICYTGDILNSARPKYDLKYYTDLAVELEKAGAHIIALKDMAGLLKPAAAKVLFKALREATGLPIHFHTHDTSGIAAATVLAAVDAGVDAVDAAMDALSGNTSQPCLGSIVEALKGSERDPGLDPEWIRRISFYWEAVRHQYAAFESDLKGPASEVYLHEMPGGQFTNLKEQARSLGLETRWHKVAQAYADANQMFGDIVKVTPSSKVVGDMALMMVSQDLTVADVENPAKDIAFPDSVVSMLKGDLGQPPSGWPQALQKKALKGDTPYTVRPGSLLAEADLDAERKVIETKLERKVDDFEFASYLMYPKVFTDYALAADTYGPVSVLPTPAYFYGLKEGDELFAEIEKGKTLVIVNQAMTATDEKGMVTVFFELNGQPRRIKVPDRAHGASGAAIRRKAETGNAAHVGAPMPGVISTVFVSPGQAIKAGDVLVSIEAMKMETALHAEKDGTISEVLVRAGDQIDAKDLLVVYGA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QERI01000011
EMBL· GenBank· DDBJ
TGE94909.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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