ID   ALLA_SALEN              Reviewed;         160 AA.
AC   Q9S4Y6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 93.
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}; Synonyms=glxA2;
OS   Salmonella enteritidis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=149539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=S1400;
RX   PubMed=10447888; DOI=10.1046/j.1365-2958.1999.01526.x;
RA   Pattery T., Hernalsteens J.-P., De Greve H.;
RT   "Identification and molecular characterization of a novel Salmonella
RT   enteritidis pathogenicity islet encoding an ABC transporter.";
RL   Mol. Microbiol. 33:791-805(1999).
CC   -!- FUNCTION: Catalyzes the catabolism of the allantoin degradation
CC       intermediate (S)-ureidoglycolate, generating urea and glyoxylate.
CC       Involved in the utilization of allantoin as nitrogen source.
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; AF102556; AAD51884.1; -; Genomic_DNA.
DR   RefSeq; WP_000764661.1; NZ_WIAP01000024.1.
DR   AlphaFoldDB; Q9S4Y6; -.
DR   SMR; Q9S4Y6; -.
DR   PATRIC; fig|149539.316.peg.535; -.
DR   OMA; WNIFRCS; -.
DR   UniPathway; UPA00395; -.
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_0000120557"
SQ   SEQUENCE   160 AA;  18139 MW;  A4579B306F801E51 CRC64;
     MKLEVLPLDQ KTFSAYGDVI ETQERDFFHI NNGLVERYHD LAKVEVLEQD RTLISINRAQ
     PAAMPIVVHE LERHPLGTQA FVPMNGEAFV VIVALGDDKP ELSTLRAFIS NGRQGVNYHR
     NVWHHPLFAW QTVTDFLTVD RGGSDNCDVE SIPTHELCFA