A0A2S8JYT1 · A0A2S8JYT1_ECOLX

  • Protein
    Allantoinase
  • Gene
    allB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 Zn2+ ions per subunit.

Pathway

Nitrogen metabolism; (S)-allantoin degradation; allantoate from (S)-allantoin: step 1/1.

Features

Showing features for binding site.

145350100150200250300350400450
TypeIDPosition(s)Description
Binding site59Zn2+ 1 (UniProtKB | ChEBI)
Binding site61Zn2+ 1 (UniProtKB | ChEBI)
Binding site146Zn2+ 1 (UniProtKB | ChEBI); via carbamate group
Binding site146Zn2+ 2 (UniProtKB | ChEBI); via carbamate group
Binding site186Zn2+ 2 (UniProtKB | ChEBI)
Binding site242Zn2+ 2 (UniProtKB | ChEBI)
Binding site315Zn2+ 1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionallantoinase activity
Molecular Functioncobalt ion binding
Molecular Functionzinc ion binding
Biological Processallantoin catabolic process
Biological Processpurine nucleobase catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Allantoinase
  • EC number
  • Alternative names
    • Allantoin-utilizing enzyme

Gene names

    • Name
      allB
    • ORF names
      NCTC10082_00955

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • NCTC10082
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    A0A2S8JYT1

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue146N6-carboxylysine

Post-translational modification

Carboxylation allows a single lysine to coordinate two zinc ions.

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain50-431Amidohydrolase-related

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    453
  • Mass (Da)
    49,530
  • Last updated
    2018-07-18 v1
  • Checksum
    3099386081CA3C00
MSFDLIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGDAKDVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHELDEVGVVGFKCFVATCGDRGIDNDFRDVNDWQFFKGAQKLGELGQPVLVHCENALICDALGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVCHVSSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEKIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMEAWGGIAGLQSCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFILKHQQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
UFZA01000001
EMBL· GenBank· DDBJ
STE02651.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp