ID   UGL_BURM1               Reviewed;         282 AA.
AC   A9ALD1;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Bmul_3283, BMULJ_05242;
OS   Burkholderia multivorans (strain ATCC 17616 / 249).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=395019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia multivorans ATCC
RT   17616.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA   Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA   Hattori M., Tsuda M.;
RT   "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL   Submitted (APR-2007) 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; CP000869; ABX16967.1; -; Genomic_DNA.
DR   EMBL; AP009386; BAG47080.1; -; Genomic_DNA.
DR   RefSeq; WP_012216272.1; NC_010805.1.
DR   AlphaFoldDB; A9ALD1; -.
DR   SMR; A9ALD1; -.
DR   STRING; 395019.Bmul_3283; -.
DR   EnsemblBacteria; BAG47080; BAG47080; BMULJ_05242.
DR   KEGG; bmj:BMULJ_05242; -.
DR   KEGG; bmu:Bmul_3283; -.
DR   eggNOG; COG0179; Bacteria.
DR   HOGENOM; CLU_028458_3_4_4; -.
DR   OMA; YVSQCMS; -.
DR   UniPathway; UPA00394; -.
DR   Proteomes; UP000008815; 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; Reference proteome.
FT   CHAIN           1..282
FT                   /note="Ureidoglycolate lyase"
FT                   /id="PRO_0000371515"
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;  30170 MW;  C84E1944DAC890D8 CRC64;
     MKLLRYGPPG QEKPGILDAD GRIRDLSAHV PDLAGDVLSD AGLARLRALD PATLPLVSGE
     PRIGACVGRV GKFIGIGLNY ADHAAEAGMP VPKEPVVFGK WTSSICGPND GIDIPKGSVK
     TDWEVELGVV IGAPCKDVDE ARALDYVAGY CVVNDVSERE WQIERGGQWD KGKGFDTFGP
     IGPWLVTRDE VPDPQSLDLW LEVDGHRYQN GNTRTMVFTV AQLIAYLSSC MTLQPGDVIT
     TGTPPGVGMG IKPAPVYLKA GQMVRLGIEG LGEQLQLTRA AR