A0A1V8RN46 · A0A1V8RN46_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.

TypeIDPosition(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
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
      BFN67_21415

Organism names

  • Taxonomic identifier
  • Strain
    • JH-7
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Phyllobacteriaceae > Pseudaminobacter

Accessions

  • Primary accession
    A0A1V8RN46

Proteomes

PTM/Processing

Features

Showing features for modified residue.

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

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, compositional bias, region.

TypeIDPosition(s)Description
Domain2-462Biotin carboxylation
Domain128-326ATP-grasp
Domain539-807Pyruvate carboxyltransferase
Compositional bias1063-1082Basic and acidic residues
Region1063-1083Disordered
Domain1077-1152Lipoyl-binding

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,152
  • Mass (Da)
    126,367
  • Last updated
    2017-06-07 v1
  • Checksum
    FC099351A3C9AC2F
MPISKILVANRSEIAIRVFRAANELGLKTVAIWAEEDKYSLHRFKADESYQVGRGPWLTKDMGPIESYLSIEEVLRVAKLSGADAIHPGYGLLSESPEFADACAKAGITFIGPAPKTMRRLGNKVAARNLAIEVGVPVVPATEPLPDDMEAVKKLAAQIGYPVMLKASWGGGGRGMRAIRSEADLAREVIEGKREAKAAFGKDEVYLEKLIERARHVEVQVLGDKHGNVVHLYERDCSIQRRNQKVVERAPAPYLDAAQREELCGYALRIARETSYVGAGTVEFLMDADSGKFYFIEVNPRIQVEHTVTEEVTGIDIVKAQIHILDGHAIGTPQSGVPAQMDIRLNGHALQCRITTEDPEHNFIPDYGRITAYRGATGFGIRLDGGTAYSGAVITRFYDPLLEKVTAWAPTSGETIARMNRALREFRIRGVATNLTFLEAIIRHPDFANNSYTTRFIDNTPELFSHVRRQDRATKLLNYLGDVTVNGHPEARGRPQPKADAAMPVIPWFTGPIADGMKQRLDALGPEKFSRWMREQDKVLVTDTTMRDGHQSLLATRVRTHDIARIAGTYARALPQLLSLECWGGATFDVAMRFLTEDPWERLAMIRKAAPNILLQMLLRGANGVGYTNYPDNVVRYFVTEAARGGVDLFRVFDCLNWVENMRVAMDAVASEGKLVEAAMCYTGDILDPERAKYDLKYYIGLAKELEAAGAHILAVKDMSGLLKPAAARVLFKALREATDLPIHFHTHDTSGLSAATVLAAVEAGVDAIDAAMDPFSGNTSQPCLGSIIEALKGSDRAPDLDPEWIRRISFYWEAVRNQYAAFESDLKGPASEVYLHEMPGGQFTNLKEQARSLGLEMRWHEVAQAYHDVNLMFGDIVKVTPSSKVVGDMALMMVSQDLSIADVENPAKDIAFPDSVVAMLHGDLGQSPGGWPEKLQKKVLKGGKPITVRPGSLLKPADLDAERKMISDKLGRSLSNQEFASWLMYPKVFSDFAAAQESYGPVSVLPTPSYFYGMKPADEIFLDLEKGKTLVVRCLGIGDADDKGMVTVFFELNGQPRRVKVPDRTHGAGAAKARRKAEPGNDAHVAAPMPGVVSAVPVVAGQAVRAGDVLLSIEAMKMETALHAERDGVIAEVLARAGDQIDAKDLLIVYG

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1063-1082Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MDET01000027
EMBL· GenBank· DDBJ
OQM74576.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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