ID   ALLA_PSEPW              Reviewed;         167 AA.
AC   B1JC20;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Ureidoglycolate lyase {ECO:0000255|HAMAP-Rule:MF_00616};
DE            EC=4.3.2.3 {ECO:0000255|HAMAP-Rule:MF_00616};
DE   AltName: Full=Ureidoglycolatase {ECO:0000255|HAMAP-Rule:MF_00616};
GN   Name=allA {ECO:0000255|HAMAP-Rule:MF_00616};
GN   OrderedLocusNames=PputW619_3614;
OS   Pseudomonas putida (strain W619).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=390235;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W619;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA   Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA   Richardson P.;
RT   "Complete sequence of Pseudomonas putida W619.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the catabolism of the allantoin degradation
CC       intermediate (S)-ureidoglycolate, generating urea and glyoxylate.
CC       Involved in the utilization of allantoin as nitrogen source.
CC       {ECO:0000255|HAMAP-Rule:MF_00616}.
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:0000255|HAMAP-Rule:MF_00616};
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00616};
CC   -!- PATHWAY: Nitrogen metabolism; (S)-allantoin degradation.
CC       {ECO:0000255|HAMAP-Rule:MF_00616}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00616}.
CC   -!- SIMILARITY: Belongs to the ureidoglycolate lyase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00616}.
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DR   EMBL; CP000949; ACA74096.1; -; Genomic_DNA.
DR   RefSeq; WP_012315446.1; NC_010501.1.
DR   AlphaFoldDB; B1JC20; -.
DR   SMR; B1JC20; -.
DR   STRING; 390235.PputW619_3614; -.
DR   EnsemblBacteria; ACA74096; ACA74096; PputW619_3614.
DR   KEGG; ppw:PputW619_3614; -.
DR   eggNOG; COG3194; Bacteria.
DR   HOGENOM; CLU_070848_1_0_6; -.
DR   OMA; WNIFRCS; -.
DR   OrthoDB; 1597997at2; -.
DR   UniPathway; UPA00395; -.
DR   GO; GO:0004848; F:ureidoglycolate hydrolase activity; IEA:InterPro.
DR   GO; GO:0050385; F:ureidoglycolate lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000256; P:allantoin catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006145; P:purine nucleobase catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.120.480; -; 1.
DR   HAMAP; MF_00616; Ureidogly_lyase; 1.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   InterPro; IPR007247; Ureidogly_lyase.
DR   InterPro; IPR023525; Ureidogly_lyase_bac.
DR   InterPro; IPR024060; Ureidoglycolate_lyase_dom_sf.
DR   PANTHER; PTHR21221; PTHR21221; 1.
DR   Pfam; PF04115; Ureidogly_lyase; 1.
DR   PIRSF; PIRSF017306; Ureidogly_hydro; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   3: Inferred from homology;
KW   Lyase; Purine metabolism.
FT   CHAIN           1..167
FT                   /note="Ureidoglycolate lyase"
FT                   /id="PRO_1000130419"
SQ   SEQUENCE   167 AA;  18722 MW;  4DA3B0335A3818D2 CRC64;
     MRTLMIEPLT KEAFAPFGDV IETDGSDHFM INNGSTMRFH KLATVETAEP EDKAIISIFR
     ADALDMPLTV RMLERHPLGS QAFIPLLGNP FLIVVAPVGD APVSGLVRAF RSNGRQGVNY
     HRGVWHHPVL TIEKRDDFLV VDRSGSGNNC DEHYFTEEQM LILNPHQ