A0A2B7WKJ6 · A0A2B7WKJ6_POLH7

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.
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.

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 site162ATP (UniProtKB | ChEBI)
Binding site246ATP (UniProtKB | ChEBI)
Binding site281ATP (UniProtKB | ChEBI)
Active site338
Binding site591Mn2+ (UniProtKB | ChEBI)
Binding site663substrate
Binding site759Mn2+ (UniProtKB | ChEBI); via carbamate group
Binding site789Mn2+ (UniProtKB | ChEBI)
Binding site791Mn2+ (UniProtKB | ChEBI)
Binding site924substrate

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
      AJ80_09748

Organism names

  • Taxonomic identifier
  • Strain
    • UAMH7299
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Onygenales > Onygenales incertae sedis > Polytolypa

Accessions

  • Primary accession
    A0A2B7WKJ6

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue759N6-carboxylysine
Modified residue1160N6-biotinyllysine

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain44-496Biotin carboxylation
Domain166-363ATP-grasp
Domain582-850Pyruvate carboxyltransferase
Domain1119-1194Lipoyl-binding

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,197
  • Mass (Da)
    131,248
  • Last updated
    2017-12-20 v1
  • Checksum
    E72FDDC3ECBC0BE1
MSSLGDSKPVVVDEAVEDIVEDHSHHDPAHSVHRRLRANSTIMRFNKILVANRGEIPIRIFRTAHELSLQTVAVYSYEDRLSMHRQKADEAYVIGTRGQYTPVGAYLAGDEIIKIALQHDVQLIHPGYGFLSENAAFARNVERAGLVFVGPTPDTIEALGDKVSARQLAIKCGVPVVPGTPGPVERFEEVKAFTDEYGFPIIIKAAFGGGGRGMRVVRDQESLSESFERATSEAKSAFGNGTVFVERFLDKPKHIEVQLLGDNHGNVVHLYERDCSVQRRHQKVVEIAPAKDLPVEVRDSILADAVKLAKSVDYRNAGTAEFLVDQMNRYYFIEINPRIQVEHTITEEITGIDVVAAQIQIAAGATLEQLGLTQDRITTRGFAIQCRITTEDPSKGFSPDTGKIEVYRSAGGNGVRLDGGNGFAGAIITPHYDSMLVKCTCHGSTYEIVRRKMLRALVEFRIRGVKTNIPFLASLLTHPTFIDGNCWTTFIDDSPELFSMIGSQNRAQKLLAYLGDVAVNGSSIKGQIGEPKFKGEISMPTIVDENDNPIDVTFPCTDGWKQVLDEEGPEGFAKAIRANKGCLIMDTTWRDAHQSLLATRVRTVDLVNIAKETSYAYSNAYSLECWGGATFDVAMRFLYEDPWDRLRKLRKAVPNIPFQMLLRGANGVAYSSLPDNAIYHFCKQAKKYGVDIFRVFDALNDINQLEVGMKAVAAAGGVIEATICYSGDMLNPKKKYNLQYYLDLADKIVKVGTHILGIKDMAGVLKPRAATLLIGAIRERYPDLPIHVHTHDSAGTGVASMVACAQAGADAVDAATDSLSGMTSQPSVGAILASLEGTEFDPNLNTQNIRAIDSYWAQLRLLYSPFEAGLTGPDPEVYEHEIPGGQLTNLIFQAHQLGLGKQWAQTKKAYEQANDLLGDIVKVTPTSKVVGDLAQFMVSNKLTPDDVVARAGELDFPASVLEFLEGLMGQPYGGFPEPLRTRALRERRKLDTRPGLHLPALDLAQIKADLKEKFGTSTECDVASFAMYPKVFEDYRKFVAKYGDLSVLPTKYFLTRPEIGEEFAVELEQGKVLILKLLAIGPLSEQTGLREVFYEMNGEVRQVSVDDKLASVDNATRPKADPLDSSQVGAPMSGVVVEIRANDGLEVKKGDPIAVLSAMKMEMVISAPHHGVVSGLLVKEGDSVDGQDLICRITKPA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PDNA01000335
EMBL· GenBank· DDBJ
PGG97068.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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