UGL_BURCH
ID UGL_BURCH Reviewed; 282 AA.
AC A0B3M8;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=Bcen2424_5521;
OS Burkholderia cenocepacia (strain HI2424).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=331272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI2424;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., LiPuma J.J., Gonzalez C.F.,
RA Konstantinidis K., Tiedje J.M., Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia cenocepacia HI2424.";
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; CP000459; ABK12254.1; -; Genomic_DNA.
DR RefSeq; WP_011548908.1; NC_008543.1.
DR AlphaFoldDB; A0B3M8; -.
DR SMR; A0B3M8; -.
DR KEGG; bch:Bcen2424_5521; -.
DR HOGENOM; CLU_028458_3_4_4; -.
DR OMA; YVSQCMS; -.
DR OrthoDB; 775108at2; -.
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_0000371510"
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