ID   UGL_BURL3               Reviewed;         282 AA.
AC   Q39BA7;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Bcep18194_B0137;
OS   Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS   R18194 / 383).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=482957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia sp. 383.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 1-42; 48-62 AND 197-207, PATHWAY, CATALYTIC ACTIVITY,
RP   AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=14506266; DOI=10.1074/jbc.m303828200;
RA   McIninch J.K., McIninch J.D., May S.W.;
RT   "Catalysis, stereochemistry, and inhibition of ureidoglycolate lyase.";
RL   J. Biol. Chem. 278:50091-50100(2003).
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:0000269|PubMed:14506266};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=500 uM for Ureidoglycolate {ECO:0000269|PubMed:14506266};
CC         Vmax=180 mmol/min/mg enzyme {ECO:0000269|PubMed:14506266};
CC   -!- PATHWAY: Purine metabolism; urate degradation.
CC       {ECO:0000269|PubMed:14506266}.
CC   -!- SIMILARITY: Belongs to the FAH family. {ECO:0000305}.
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; CP000152; ABB10254.1; -; Genomic_DNA.
DR   RefSeq; WP_011353752.1; NZ_CABVQI010000024.1.
DR   AlphaFoldDB; Q39BA7; -.
DR   SMR; Q39BA7; -.
DR   EnsemblBacteria; ABB10254; ABB10254; Bcep18194_B0137.
DR   GeneID; 45096525; -.
DR   KEGG; bur:Bcep18194_B0137; -.
DR   PATRIC; fig|482957.22.peg.3706; -.
DR   HOGENOM; CLU_028458_3_4_4; -.
DR   OMA; YVSQCMS; -.
DR   OrthoDB; 775108at2; -.
DR   SABIO-RK; Q39BA7; -.
DR   UniPathway; UPA00394; -.
DR   Proteomes; UP000002705; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Lyase; Metal-binding; Nucleotide metabolism.
FT   CHAIN           1..282
FT                   /note="Ureidoglycolate lyase"
FT                   /id="PRO_0000371508"
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;  30298 MW;  2ED0C9C30A1093E2 CRC64;
     MKLLRYGPSG QEKPGILDAD GRIRDLSAHV PDLSGDVLSD AGLARLRAID PATLPLVSGE
     PRIGACVGHV GKFIGIGLNY ADHAAEAGMP VPKEPVVFGK WTSSICGPND GIDIPKGSVK
     TDWEVELGVV IGATCKDVDE ARALDYVAGY CVVNDVSERE WQIERGGQWD KGKGFDTFGP
     IGPWLVTRDE VPDPQRLDLW LEIDGHRYQN GNTRTMVFTV AQLIAYLSSC MTLQPGDVIT
     TGTPPGVGMG IKPSPVFLKA GQMVRLGVEG LGEQLQHTRD AR