O93918 · PYC_ASPTE

  • Protein
    Pyruvate carboxylase
  • Gene
    pyc
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    3/5

Function

function

Pyruvate carboxylase 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

Protein has several cofactor binding sites:
biotin (UniProtKB | Rhea| CHEBI:57586 )

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Pathway

Carbohydrate biosynthesis; gluconeogenesis.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site159ATP (UniProtKB | ChEBI)
Binding site243ATP (UniProtKB | ChEBI)
Binding site278ATP (UniProtKB | ChEBI)
Active site335
Binding site587-591substrate
Binding site588a divalent metal cation (UniProtKB | ChEBI)
Binding site660substrate
Binding site756a divalent metal cation (UniProtKB | ChEBI); via carbamate group
Binding site786a divalent metal cation (UniProtKB | ChEBI)
Binding site788a divalent metal cation (UniProtKB | ChEBI)
Binding site921substrate

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
  • Alternative names
    • Pyruvic carboxylase (PCB)

Gene names

    • Name
      pyc

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati

Accessions

  • Primary accession
    O93918

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001468201-1193Pyruvate carboxylase
Modified residue756N6-carboxylysine
Modified residue1157N6-biotinyllysine

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain41-493Biotin carboxylation
Domain163-360ATP-grasp
Domain579-847Pyruvate carboxyltransferase
Domain1116-1191Biotinyl-binding

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,193
  • Mass (Da)
    131,222
  • Last updated
    1999-05-01 v1
  • Checksum
    6E24E000CE793206
MAAPYRQPEEAVDDSEFIDDHHDHLRDTVHHRLRANSAIMQFQKILVANRGEIPIRIFRTAHELSLQTVAIFSHEDRLSMHRQKADEAYMIGHRGQYTPVGAYLAADEIVKIALEHGVHLIHPGYGFLSENADFARKVEKAGMVFVGPTPDTIDSLGDKVSARQLAIRCNVPVVPGTEGPVERYEEVKAFTDTYGFPIIIKAAFGGGGRGMRVVRNQADLRDSFERATSEARSAFGNGTVFVERFLDKPKHIEVQLLGDNHGNVVHLFERDCSVQRRHQKVVEVAPAKDLPTDVRDRILSDAVKLAKSVNYRNAGTAEFLVDQQNRHYFIEINPRIQVEHTITEEITGIDIVAAQIQIAAGATLEQLGLTQDRISTRGFAIQCRITTEDPSKGFSPDTGKIEVYRSAGGNGVRLDGGNGFAGAIITPHYDSMLVKCTCRGSTYEIARRKVVRALVEFRIRGVKTNIPFLTSLLSHPTFVDGNCWTTFIDDTPELFALVGSQNRAQKLLAYLGDVAVNGSSIKGQMGEPKFKGEIIKPKLLDAQGKPLDVSQPCTKGWKQIIDQEGPVAFAKAVRANKGCLIMDTTWRDAHQSLLATRVRTIDLLNIAHETSHALSNAYSLECWGGATFDVAMRFLYEDPWDRLRKMRKAVPNIPFQMLLRGANGVAYSSLPDNAIYHFCKNAKKCGVDIFRVFDALNDIDQLEVGIKAVHAAEGVVEATVCYSGDMLNPKKKYNLEYYLALVDKIVALKPHVLGIKDMAGVLKPQAARLLVGSIRERYPDLPIHVHTHDSAGTGVASMIACAQAGADAVDAATDSMSGMTSQPSIGAILASLEGTEHDPGLNSAHVRALDSYWAQLRLLYSPFEANLTGPDPEVYEHEIPGGQLTNLIFQASQLGLGQQWAETKKAYEVANDLLGDIVKVTPTSKVVGDLAQFIVSNKLSAQDVVDRAAELDFPGSVLEFLEGLMGQPFGGFPEPLRSRALRNRRKLDKRPGLYLEPLDLAAIKNQIREQFGSATEYDVASYAMYPKVFEDYKKFVQKYGDLSVLPTRYFLAKPEIGEEFHVELEKGKVLILKLLAIGPLSEQTGQREVFYEVNGEVRQVSIDDKKASIDNTARPKADVGDSSQVGAPMSGVVVEIRVHDGLEVKKGDPLAVLSAMKMEMVISAPHSGKVSGLLVKEGDSVDGQDLVCKITKA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF097728
EMBL· GenBank· DDBJ
AAC69197.1
EMBL· GenBank· DDBJ
mRNA

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