ALLA_ECO24
ID ALLA_ECO24 Reviewed; 160 AA.
AC A7ZIR2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=EcE24377A_0542;
OS Escherichia coli O139:H28 (strain E24377A / ETEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331111;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E24377A / ETEC;
RX PubMed=18676672; DOI=10.1128/jb.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic analysis
RT of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(2008).
CC -!- FUNCTION: Catalyzes the catabolism of the allantoin degradation
CC intermediate (S)-ureidoglycolate, generating urea and glyoxylate.
CC Involved in the anaerobic utilization of allantoin as sole nitrogen
CC source. Reinforces the induction of genes involved in the degradation
CC of allantoin and glyoxylate by producing glyoxylate.
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; CP000800; ABV17202.1; -; Genomic_DNA.
DR RefSeq; WP_000776392.1; NC_009801.1.
DR AlphaFoldDB; A7ZIR2; -.
DR SMR; A7ZIR2; -.
DR EnsemblBacteria; ABV17202; ABV17202; EcE24377A_0542.
DR KEGG; ecw:EcE24377A_0542; -.
DR HOGENOM; CLU_070848_1_1_6; -.
DR OMA; WNIFRCS; -.
DR UniPathway; UPA00395; -.
DR Proteomes; UP000001122; 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..160
FT /note="Ureidoglycolate lyase"
FT /id="PRO_1000061351"
SQ SEQUENCE 160 AA; 18249 MW; F891A4710EF92EC7 CRC64;
MKLQVLPLSQ EAFSAYGDVI ETQQRDFFHI NNGLVERYHD LALVEILEQD RTLISINRAQ
PANLPLTIYE LERHPLGTQA FIPMKGEVFV VVVALGDDKP DLSTLRAFIT NGEQGVNYHR
NVWHHPLFAW QRVTDFLTID RGGSDNCDVE SIPEQELCFA