A0A8J8W6C7 · A0A8J8W6C7_9EURO

  • Protein
    Bifunctional pyrimidine biosynthesis protein (PyrABCN)
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

Caution

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

Catalytic activity

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site339Nucleophile
Active site423
Active site425

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionamino acid binding
Molecular Functionaspartate carbamoyltransferase activity
Molecular FunctionATP binding
Molecular Functioncarbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
Molecular Functiondihydroorotase activity
Molecular Functionmetal ion binding
Biological Process'de novo' pyrimidine nucleobase biosynthetic process
Biological Process'de novo' UMP biosynthetic process
Biological Processcitrulline biosynthetic process
Biological Processglutamine metabolic process
Biological ProcessUTP biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Submitted names
    • Bifunctional pyrimidine biosynthesis protein (PyrABCN)
      (EC:2.1.3.2
      , EC:6.3.5.5
      )

Gene names

    • ORF names
      PECM_003836

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • S1M29
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Penicillium

Accessions

  • Primary accession
    A0A8J8W6C7

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-24Disordered
Domain601-793ATP-grasp
Domain1136-1327ATP-grasp
Domain1393-1572MGS-like
Region1873-1903Disordered

Sequence similarities

In the 2nd section; belongs to the CarB family.
In the 3rd section; belongs to the metallo-dependent hydrolases superfamily. DHOase family. CAD subfamily.
In the C-terminal section; belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
In the N-terminal section; belongs to the CarA family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    2,250
  • Mass (Da)
    246,917
  • Last updated
    2022-05-25 v1
  • Checksum
    32E92692FC14F39F
MSQPASIQDSALPTSPTSGGVVGYPSTTDIASTMDAATGTMIAPASIPVRGGTDRLVALELEDGTVYQGYNFGAEKSVSGELVFQTGMVGYPESITDPSYRGQILVITFPLVGNYGVPSREQIDELLQLPTYFESSEIHVAALVVATYAGEDFSHFLAESSLGQWLKEQGVPAMHGVDTRALTKRIRQKGSMLGRMLLQNAGEANAVAGAIVGENWKSHFEQVEWVDPNKKNLVAEVSIREPKLWSPPADVALKHPSGRPVRVLCLDVGMKYNQLRCLLNRGVEVMVVPWDYDFPTLAGKDYDGLFVSNGPGDPATLSTTIENLARTLKDARTPVFGICLGHQLIARSVGATTSKMKFGNRGHNIPCTSMISGKCHITSQNHGYAVDASSLPEGWEELFVNANDASNEGIRHTSRPFFSVQFHPESTPGPRDTEYLFDVFIKTIMNTIASPETLSKPVEFPGGLKADNVKAAPRVHVKKVLVLGSGGLSIGQAGEFDYSGSQAIKALKEEGIYTILINPNIATIQTSKGLADKVYFLPVNADFVRKVIKHERPDAIYVTFGGQTALQVGIQLKDEFEGLGVKVLGTPIDTIITTEDRELFARSMDSINEKCAKSASASTLEESLRVVKDIGFPVIVRAAYALGGLGSGFAENMDELKELCTKALAVSPQVLIERSMKGWKEIEYEVVRDAQDNCITVCNMENFDPLGIHTGDSIVVAPSQTLSDEDYNMLRTTAVNVIRHLGVVGECNIQYALNPFSKEYCIIEVNARLSRSSALASKATGYPLAFIAAKLGLGIPLNEIKNSVTKSTCACFEPSLDYCVVKIPRWDLKKFTRVSTQLGSSMKSVGEVMSIGRTFEEAIQKAIRSVDYNNLGFNETEALMSLDEELQTPSDQRLFAIANAMAAGYSVDDIWKLTKIDKWFLTRLKGLSNFGKSMSTFNASSVPIAMIRQAKQLGFSDRQLAKFLSSNELAVRRKRVEAGITPIVKQIDTVAAEFPAVTNYLYLTYNASEHDLTFNDHGIMVLGSGVYRIGSSVEFDWCSVRTIRTLRQQGHKTIMVNYNPETVSTDYDEADRLYFENINLETVLDIYQLETSSGVVISMGGQTPNNIALPLHRLNVNILGTSPEMIDSAENRYKFSRMLDRIGVDQPAWKELTSIEEARTFCDKVGYPVLVRPSYVLSGAAMNTVYSEHDLANYLNQAADVSREHPVVITKYIENAKEIEMDAVARNGVMVGHFISEHVENAGVHSGDATLILPPQDLSPETVRRIEEATRKIGNALNVTGPYNIQFIAKDNDIKVIECNVRASRSFPFVSKVMGVDLIEMATKAMINIPFQEYPPTNVPKDYVGVKVPQFSFSRLSGADPVLGVEMASTGEVASFGRDKYEAYLKALLSTGFKLPKRNILFSIGSYKEKLEMLPSIQKLHQLDYNLFATAGTADFLKEHGVPVKYLEILPGEDDDIKSEYSLTQHLSNNLIDLYINLPSSNRFRRPANYMSKGYRTRRMAVDYQTPLVTNVKNAKILIEAIARHYPLNIQTGDFQTSHRTVVLPGLINIAAFVPGLTTLGSKDFEQVTKASVAAGFSMVRVMPVGVEGSITEASDLKIVQQNAQDQSYCDFNLSVAATADNSDQIVQVTGEVGSLFIPFNHLSGNINKVATVTKHFGVWPSSKPLITDAKGTDLASILLLASLHSRNIHVMSVTSKEDINLIALSKEKGLKVTCDVSIFSLFLSQDDHPACSSLPSAEDQKALWDHMSTIDVFSIGSIPYQLAGKDATPEVGIAESLPLLFSAVAEGRLTVDDVTARLHDNPKKIFELHDQADSSLEIEIDRPYVFQSPNGTWSPFNGKMMRGSVQRVVFQGKTSCLDGLLAKDAIKGSDMSTHRIVPSSPVHKPTTPMVRPESALDRHTTPSRHARARALDAAVPTVGELGPPLYAASSQVSSALSEMLSRSTFRGKHVLSVNQFTRSDLHLLFTVAQEMRLGVQRHGVLDILKGRVLATLFYEPSTRTSASFDAAMQRLGGRTIPISTEHSSTQKGETLQDTLRTLGCYADAVVLRHPEPSSTSVAAKFAQVPVINGGNGSLEHPTQAFLDLFTIREELGTVTGLTITFTGDLKYGRPVHSLIKLLQFYDVRIQLVSPKELALPGEVRQQIVASGQLVGESEELTPEIVARSDVLYSTRVQKERFADLAQYDRLKNSFIIDNALLKHAKSHMVVLHPLPRNAEIAEEVDFDQRAAYFRQMRYGLYCRMALLALVLAH

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WIWV01000023
EMBL· GenBank· DDBJ
KAF7717759.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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