Database accession: MF7001002
Name: Ureidoglycolate hydrolase (AllA) (Escherichia coli O157:H7)
PDB ID: 1yqc
Experimental method: X-ray (1.71 Å)
Assembly: Homodimer
Source organism: Escherichia coli O157:H7
Primary publication of the structure:
Raymond S, Tocilj A, Ajamian E, Li Y, Hung MN, Matte A, Cygler M
Crystal structure of ureidoglycolate hydrolase (AllA) from Escherichia coli O157:H7.
(2005) Proteins 61: 454-9
PMID: 16114032
Abstract:
Not available.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
ureidoglycolate hydrolase activity ureidoglycolate hydrolase activity
ureidoglycolate lyase activity ureidoglycolate lyase activity
Biological process:
allantoin catabolic process allantoin catabolic process
purine nucleobase catabolic process purine nucleobase catabolic process
Cellular component: not assigned
Structural annotations of the participating protein chains.Entry contents: 2 distinct polypeptide molecules
Chains: A, B
Notes: All chains according to the most probable oligomerization state stored in PDBe were considered.
Number of unique protein segments: 1
Name: Ureidoglycolate lyase
Source organism: Escherichia coli O157:H7
Length: 160 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMKLQVLPLSQEAFSAYGDVIETQQRDFFHINNGLVERYHDLALVEILEQDRTLISINRAQPANLPLTIHELERHPLGTQAFIPMKGEVFVVVVALGDDKPDLSTLRAFITNGEQGVNYHRNVWHHPLFAWQRVTDFLTIDRGGSDNCDVESIPEQELCFA
UniProtKB AC: P63486 (positions: 1-160)
Coverage: 100%
Name: Ureidoglycolate lyase
Source organism: Escherichia coli O157:H7
Length: 160 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMKLQVLPLSQEAFSAYGDVIETQQRDFFHINNGLVERYHDLALVEILEQDRTLISINRAQPANLPLTIHELERHPLGTQAFIPMKGEVFVVVVALGDDKPDLSTLRAFITNGEQGVNYHRNVWHHPLFAWQRVTDFLTIDRGGSDNCDVESIPEQELCFA
UniProtKB AC: P63486 (positions: 1-160)
Coverage: 100%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: -
Evidence level: Indirect evidence
Evidence coverage: The full structure participates in mutual synergistic folding.
Complex Evidence:
Domain-swapped dimer with beta sheet augmentation and an extensive interface. Face-to-face interactions of 5-stranded b-sheets of the two monomers. Both monomers contribute to the putative active site (PMID:16114032).
Chain A:
N/A
Chain B:
N/A
Surface and contacts features:
Structures from the PDB that contain the same number of proteins, and the proteins from the two structures show a sufficient degree of pairwise similarity, i.e. they belong to the same UniRef90 cluster (the full proteins exhibit at least 90% sequence identity) and convey roughly the same region to their respective interactions (the two regions from the two proteins share a minimum of 70% overlap). No related structure was found in the MFIB database.
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