ALLA_ECOSM
ID ALLA_ECOSM Reviewed; 160 AA.
AC B1LKC4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Ureidoglycolate lyase {ECO:0000255|HAMAP-Rule:MF_00616};
DE EC=4.3.2.3 {ECO:0000255|HAMAP-Rule:MF_00616};
DE AltName: Full=Ureidoglycolatase {ECO:0000255|HAMAP-Rule:MF_00616};
GN Name=allA {ECO:0000255|HAMAP-Rule:MF_00616};
GN OrderedLocusNames=EcSMS35_0548;
OS Escherichia coli (strain SMS-3-5 / SECEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=439855;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMS-3-5 / SECEC;
RX PubMed=18708504; DOI=10.1128/jb.00661-08;
RA Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA Ravel J., Stepanauskas R.;
RT "Insights into the environmental resistance gene pool from the genome
RT sequence of the multidrug-resistant environmental isolate Escherichia coli
RT SMS-3-5.";
RL J. Bacteriol. 190:6779-6794(2008).
CC -!- FUNCTION: Catalyzes the catabolism of the allantoin degradation
CC intermediate (S)-ureidoglycolate, generating urea and glyoxylate.
CC Involved in the anaerobic utilization of allantoin as sole nitrogen
CC source. Reinforces the induction of genes involved in the degradation
CC of allantoin and glyoxylate by producing glyoxylate.
CC {ECO:0000255|HAMAP-Rule:MF_00616}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-ureidoglycolate = glyoxylate + urea; Xref=Rhea:RHEA:11304,
CC ChEBI:CHEBI:16199, ChEBI:CHEBI:36655, ChEBI:CHEBI:57296; EC=4.3.2.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00616};
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00616};
CC -!- PATHWAY: Nitrogen metabolism; (S)-allantoin degradation.
CC {ECO:0000255|HAMAP-Rule:MF_00616}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00616}.
CC -!- SIMILARITY: Belongs to the ureidoglycolate lyase family.
CC {ECO:0000255|HAMAP-Rule:MF_00616}.
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DR EMBL; CP000970; ACB18201.1; -; Genomic_DNA.
DR RefSeq; WP_000776393.1; NC_010498.1.
DR AlphaFoldDB; B1LKC4; -.
DR SMR; B1LKC4; -.
DR EnsemblBacteria; ACB18201; ACB18201; EcSMS35_0548.
DR KEGG; ecm:EcSMS35_0548; -.
DR HOGENOM; CLU_070848_1_1_6; -.
DR OMA; WNIFRCS; -.
DR UniPathway; UPA00395; -.
DR Proteomes; UP000007011; Chromosome.
DR GO; GO:0004848; F:ureidoglycolate hydrolase activity; IEA:InterPro.
DR GO; GO:0050385; F:ureidoglycolate lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000256; P:allantoin catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006145; P:purine nucleobase catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.120.480; -; 1.
DR HAMAP; MF_00616; Ureidogly_lyase; 1.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR InterPro; IPR007247; Ureidogly_lyase.
DR InterPro; IPR023525; Ureidogly_lyase_bac.
DR InterPro; IPR024060; Ureidoglycolate_lyase_dom_sf.
DR PANTHER; PTHR21221; PTHR21221; 1.
DR Pfam; PF04115; Ureidogly_lyase; 1.
DR PIRSF; PIRSF017306; Ureidogly_hydro; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 3: Inferred from homology;
KW Lyase; Purine metabolism.
FT CHAIN 1..160
FT /note="Ureidoglycolate lyase"
FT /id="PRO_1000130417"
SQ SEQUENCE 160 AA; 18223 MW; 93E714110ABC3A96 CRC64;
MKLQVLPLSQ EAFSAYGDVI ETQQRDFFHI NNGLVERYHD LALVEILEQD RTLISINRAQ
PANLPLTLHE LERHPLGTQA FIPMKGEVFV VVVALGDDKP DLSTLRAFIT NGEQGVNYHR
NVWHHPLFAW QRVTDFLTID RGGSDNCDVE SIPEQELCFA