ALLA_PSEE4
ID ALLA_PSEE4 Reviewed; 167 AA.
AC Q1ICT0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 88.
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}; OrderedLocusNames=PSEEN1683;
OS Pseudomonas entomophila (strain L48).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=384676;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L48;
RX PubMed=16699499; DOI=10.1038/nbt1212;
RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT "Complete genome sequence of the entomopathogenic and metabolically
RT versatile soil bacterium Pseudomonas entomophila.";
RL Nat. Biotechnol. 24:673-679(2006).
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; CT573326; CAK14533.1; -; Genomic_DNA.
DR RefSeq; WP_011532943.1; NC_008027.1.
DR AlphaFoldDB; Q1ICT0; -.
DR SMR; Q1ICT0; -.
DR STRING; 384676.PSEEN1683; -.
DR EnsemblBacteria; CAK14533; CAK14533; PSEEN1683.
DR GeneID; 58769349; -.
DR KEGG; pen:PSEEN1683; -.
DR eggNOG; COG3194; Bacteria.
DR HOGENOM; CLU_070848_1_0_6; -.
DR OMA; WNIFRCS; -.
DR OrthoDB; 1597997at2; -.
DR UniPathway; UPA00395; -.
DR Proteomes; UP000000658; Chromosome.
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_1000061361"
SQ SEQUENCE 167 AA; 18732 MW; B9F2F5221E2D1978 CRC64;
MRTLMIEPLT KEAFAPFGDV IETDGSDHFM INNGSTMRFH KLATVETAEP EDKAIISIFR
ADALEMPLTV RMLERHPLGS QAFIPLLGNP FLIVVAPVGD APVSGLVRAF RSNGRQGVNY
HRGVWHHPVL TIEKRDDFLV VDRSGSGNNC DEHYFPEEQM LILNPHQ