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Information on EC 4.3.2.3 - ureidoglycolate lyase and Organism(s) Escherichia coli O157:H7 and UniProt Accession P63486

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EC Tree
     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.2 Amidine-lyases
                4.3.2.3 ureidoglycolate lyase
IUBMB Comments
This microbial enzyme is involved in the degradation of ureidoglycolate, an intermediate of purine degradation. Not to be confused with EC 3.5.1.116, ureidoglycolate amidohydrolase, which releases ammonia rather than urea.
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This record set is specific for:
Escherichia coli O157:H7
UNIPROT: P63486
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Word Map
  • 4.3.2.3
  • pituitary
  • neuropeptide
  • cooh-terminal
  • glycine-extended
  • endoproteolytic
  • alpha-hydroxylating
  • 1.14.17.3
  • prohormone
  • neurointermediate
  • corticotrope
  • ascorbate-dependent
  • glucuronyl
  • granule-associated
  • cuproenzymes
  • beta-monooxygenase
  • allantoicase
  • uteroglobin
The taxonomic range for the selected organisms is: Escherichia coli O157:H7
The enzyme appears in selected viruses and cellular organisms
Synonyms
peptidylglycine alpha-amidating monooxygenase, ugl, peptidyl-alpha-hydroxyglycine alpha-amidating lyase, ureidoglycolate lyase, ureidoglycolase, ureidoglycolate urea-lyase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(-)-ureidoglycolate urea-lyase
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lyase, ureidoglycolate
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UGL
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ureidoglycolase
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ureidoglycolatase
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ureidoglycolate hydrolase
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(S)-ureidoglycolate urea-lyase (glyoxylate-forming)
This microbial enzyme is involved in the degradation of ureidoglycolate, an intermediate of purine degradation. Not to be confused with EC 3.5.1.116, ureidoglycolate amidohydrolase, which releases ammonia rather than urea.
CAS REGISTRY NUMBER
COMMENTARY hide
9014-57-7
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ALLA_ECO57
160
0
18223
Swiss-Prot
-