ID   UGL_BURCM               Reviewed;         282 AA.
AC   Q0B628;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Ureidoglycolate lyase;
DE            Short=UGL;
DE            EC=4.3.2.3;
DE   AltName: Full=Ureidoglycolase;
DE   AltName: Full=Ureidoglycolatase;
DE   AltName: Full=Ureidoglycolate hydrolase;
GN   OrderedLocusNames=Bamb_4846;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Purine metabolism; urate degradation.
CC   -!- SIMILARITY: Belongs to the FAH family. {ECO:0000305}.
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DR   EMBL; CP000441; ABI90395.1; -; Genomic_DNA.
DR   RefSeq; WP_011659790.1; NZ_CP009799.1.
DR   AlphaFoldDB; Q0B628; -.
DR   SMR; Q0B628; -.
DR   STRING; 339670.Bamb_4846; -.
DR   EnsemblBacteria; ABI90395; ABI90395; Bamb_4846.
DR   GeneID; 44695440; -.
DR   KEGG; bam:Bamb_4846; -.
DR   PATRIC; fig|339670.21.peg.5207; -.
DR   eggNOG; COG0179; Bacteria.
DR   OMA; YVSQCMS; -.
DR   UniPathway; UPA00394; -.
DR   Proteomes; UP000000662; Chromosome 2.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050385; F:ureidoglycolate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019628; P:urate catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.850.10; -; 1.
DR   InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR   InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR   Pfam; PF01557; FAA_hydrolase; 1.
DR   SUPFAM; SSF56529; SSF56529; 1.
PE   3: Inferred from homology;
KW   Lyase; Metal-binding; Nucleotide metabolism.
FT   CHAIN           1..282
FT                   /note="Ureidoglycolate lyase"
FT                   /id="PRO_0000371514"
FT   BINDING         124
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   282 AA;  30236 MW;  F617003F7BB963B2 CRC64;
     MKLLRYGPSG QEKPGILDAN GRIRDLSAHV PDLAGDALSD AGLTRLRAID PATLPLVSGE
     PRIGACVGRV GKFIGIGLNY ADHAAEAGMP VPKEPVVFGK WTSSICGPND GIDIPKGSVK
     TDWEVELGVV IGTTCKDVDE ARALDYVAGY CVVNDVSERE WQIERGGQWD KGKGFDTFGP
     IGPWLVTRDE VPDPQRLDLW LEVDGHRYQN GNTRTMVFTV AQLVAYLSTC MTLQPGDVIT
     TGTPPGVGMG IKPSPVFLKA GQTVRLGIDG LGEQLQSTRN AR