ID   ALLA_PSEA8              Reviewed;         169 AA.
AC   B7UW34;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 66.
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}; OrderedLocusNames=PLES_38961;
OS   Pseudomonas aeruginosa (strain LESB58).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=557722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LESB58;
RX   PubMed=19047519; DOI=10.1101/gr.086082.108;
RA   Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I.,
RA   Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A.,
RA   Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D.,
RA   Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.;
RT   "Newly introduced genomic prophage islands are critical determinants of in
RT   vivo competitiveness in the Liverpool epidemic strain of Pseudomonas
RT   aeruginosa.";
RL   Genome Res. 19:12-23(2009).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FM209186; CAW28639.1; -; Genomic_DNA.
DR   RefSeq; WP_003083329.1; NC_011770.1.
DR   AlphaFoldDB; B7UW34; -.
DR   SMR; B7UW34; -.
DR   KEGG; pag:PLES_38961; -.
DR   HOGENOM; CLU_070848_1_0_6; -.
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..169
FT                   /note="Ureidoglycolate lyase"
FT                   /id="PRO_1000130418"
SQ   SEQUENCE   169 AA;  18983 MW;  2B67E8E345B5F980 CRC64;
     MRTLKIEPLT KEAFAPFGDV IETAGSDYFM INNGSTRRYH KLATVETAQP EDNAIISIFS
     AEKLEMPLRI RMLERHPLGS QAFIPLLGNP FLVVVAPLGD VPVPGLVRAF LTNGRQGVNY
     HRGVWHHPVL TIEKRDDFLV VDRSGSGNNC DEHFFTEDEQ LLLDPQSNQ