Q3T9S7 · Q3T9S7_MOUSE

  • Protein
    Pyruvate carboxylase
  • Gene
    Pcx
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    3/5

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.

111791002003004005006007008009001,0001,100
Type
IDPosition(s)Description
Binding site153ATP (UniProtKB | ChEBI)
Binding site237ATP (UniProtKB | ChEBI)
Binding site272ATP (UniProtKB | ChEBI)
Active site329
Binding site573Mn2+ (UniProtKB | ChEBI)
Binding site645substrate
Binding site742Mn2+ (UniProtKB | ChEBI); via carbamate group
Binding site772Mn2+ (UniProtKB | ChEBI)
Binding site774Mn2+ (UniProtKB | ChEBI)
Binding site909substrate

GO annotations

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

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Pyruvate carboxylase
  • EC number

Gene names

    • Name
      Pcx

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • NOD
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q3T9S7

Organism-specific databases

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue742N6-carboxylysine
Modified residue1145N6-biotinyllysine

Proteomic databases

PTM databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain37-487Biotin carboxylation
Domain157-354ATP-grasp
Domain564-833Pyruvate carboxyltransferase
Domain1110-1179Lipoyl-binding

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,179
  • Mass (Da)
    129,860
  • Last updated
    2005-10-11 v1
  • Checksum
    6B90E57D3F48C50F
MMLKFQTVRGGLRLLGVRRSSSAPVASPNVRRLEYKPIKRVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGLAPVQAYLHIPDIIKVAKENGVDAVHPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDSPISSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVEIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRSLPDLGLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISPHYDSLLVKVIAHGKDHPTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGTVDTQFIDENPELFQLRPAQNRAQKLLHYLGHVMVNGPTTPIPVNVSPSPVDPAVPVVPIGPPPAGFRDILLREGPEGFARAVRNHQGLLLMDTTFRDAHQSLLATRVRTHDLKKIAPYVAHNFNKLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAVDSMSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDCTATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGIPHGGFPEPFRSKVLKDLPRIEGRPGASLPPLNLKELEKDLIDRHGEEVTPEDVLSAAMYPDVFAQFKDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNRAGQRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDIKVAAGDKVAKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK172320
EMBL· GenBank· DDBJ
BAE42943.1
EMBL· GenBank· DDBJ
mRNA

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