UGL_BURCA
ID UGL_BURCA Reviewed; 282 AA.
AC Q1BJJ1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=Bcen_5340;
OS Burkholderia cenocepacia (strain AU 1054).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=331271;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU 1054;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., LiPuma J.J., Konstantinidis K.,
RA Tiedje J.M., Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia cenocepacia AU 1054.";
RL Submitted (MAY-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; CP000379; ABF80214.1; -; Genomic_DNA.
DR RefSeq; WP_011548908.1; NC_008061.1.
DR AlphaFoldDB; Q1BJJ1; -.
DR SMR; Q1BJJ1; -.
DR EnsemblBacteria; ABF80214; ABF80214; Bcen_5340.
DR KEGG; bcn:Bcen_5340; -.
DR HOGENOM; CLU_028458_3_4_4; -.
DR OMA; YVSQCMS; -.
DR UniPathway; UPA00394; -.
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_0000371509"
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; 30225 MW; EDE65AD8E0120CF5 CRC64;
MKLLRYGPSG QEKPGILDAA GRIRDLSAHV PDLAGDVLSD AGLARLRAID PATLPLVSGE
PRIGACVGHV GKFIGIGLNY ADHAAEAGMP VPKEPVVFGK WTSSICGPND GIDIPKGSVK
TDWEVELGVV IGAKCKDVDE ARALDYVAGY CVVNDVSERE WQIERGGQWD KGKGFDTFGP
IGPWLVTRDE VPDPQRLDLW LEIDGHRYQN GNTRTMVFTV AQLVAYLSTC MTLQPGDVIT
TGTPPGVGMG VKPSPVFLKA GQTVRLGIEG LGEQLQRTRD AQ