ID   ALLA_ECO57              Reviewed;         160 AA.
AC   P63486; Q8XCX8;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=Z0659, ECs0566;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH GLYOXYLATE, AND
RP   SUBUNIT.
RX   PubMed=16114032; DOI=10.1002/prot.20537;
RA   Raymond S., Tocilj A., Ajamian E., Li Y., Hung M.-N., Matte A., Cygler M.;
RT   "Crystal structure of ureidoglycolate hydrolase (AllA) from Escherichia
RT   coli O157:H7.";
RL   Proteins 61:454-459(2005).
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       ECO:0000269|PubMed:16114032}.
CC   -!- SIMILARITY: Belongs to the ureidoglycolate lyase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00616}.
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DR   EMBL; AE005174; AAG54861.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33989.1; -; Genomic_DNA.
DR   PIR; A85550; A85550.
DR   PIR; F90699; F90699.
DR   RefSeq; NP_308593.1; NC_002695.1.
DR   RefSeq; WP_000776388.1; NZ_SWKA01000005.1.
DR   PDB; 1YQC; X-ray; 1.71 A; A/B=1-160.
DR   PDBsum; 1YQC; -.
DR   AlphaFoldDB; P63486; -.
DR   SMR; P63486; -.
DR   STRING; 155864.EDL933_0590; -.
DR   EnsemblBacteria; AAG54861; AAG54861; Z0659.
DR   EnsemblBacteria; BAB33989; BAB33989; ECs_0566.
DR   GeneID; 58462776; -.
DR   GeneID; 915530; -.
DR   KEGG; ece:Z0659; -.
DR   KEGG; ecs:ECs_0566; -.
DR   PATRIC; fig|386585.9.peg.674; -.
DR   eggNOG; COG3194; Bacteria.
DR   HOGENOM; CLU_070848_1_1_6; -.
DR   OMA; WNIFRCS; -.
DR   BRENDA; 4.3.2.3; 2026.
DR   UniPathway; UPA00395; -.
DR   EvolutionaryTrace; P63486; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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   1: Evidence at protein level;
KW   3D-structure; Lyase; Purine metabolism; Reference proteome.
FT   CHAIN           1..160
FT                   /note="Ureidoglycolate lyase"
FT                   /id="PRO_0000120549"
FT   STRAND          2..7
FT                   /evidence="ECO:0007829|PDB:1YQC"
FT   HELIX           10..13
FT                   /evidence="ECO:0007829|PDB:1YQC"
FT   TURN            14..16
FT                   /evidence="ECO:0007829|PDB:1YQC"
FT   STRAND          17..20
FT                   /evidence="ECO:0007829|PDB:1YQC"
FT   STRAND          27..30
FT                   /evidence="ECO:0007829|PDB:1YQC"
FT   TURN            31..34
FT                   /evidence="ECO:0007829|PDB:1YQC"
FT   STRAND          35..43
FT                   /evidence="ECO:0007829|PDB:1YQC"
FT   STRAND          46..48
FT                   /evidence="ECO:0007829|PDB:1YQC"
FT   HELIX           49..51
FT                   /evidence="ECO:0007829|PDB:1YQC"
FT   STRAND          53..59
FT                   /evidence="ECO:0007829|PDB:1YQC"
FT   STRAND          67..73
FT                   /evidence="ECO:0007829|PDB:1YQC"
FT   STRAND          79..86
FT                   /evidence="ECO:0007829|PDB:1YQC"
FT   STRAND          90..94
FT                   /evidence="ECO:0007829|PDB:1YQC"
FT   STRAND          97..99
FT                   /evidence="ECO:0007829|PDB:1YQC"
FT   STRAND          106..109
FT                   /evidence="ECO:0007829|PDB:1YQC"
FT   STRAND          115..118
FT                   /evidence="ECO:0007829|PDB:1YQC"
FT   STRAND          129..132
FT                   /evidence="ECO:0007829|PDB:1YQC"
FT   STRAND          134..140
FT                   /evidence="ECO:0007829|PDB:1YQC"
FT   STRAND          148..158
FT                   /evidence="ECO:0007829|PDB:1YQC"
SQ   SEQUENCE   160 AA;  18223 MW;  E39014610FE93FC6 CRC64;
     MKLQVLPLSQ EAFSAYGDVI ETQQRDFFHI NNGLVERYHD LALVEILEQD RTLISINRAQ
     PANLPLTIHE LERHPLGTQA FIPMKGEVFV VVVALGDDKP DLSTLRAFIT NGEQGVNYHR
     NVWHHPLFAW QRVTDFLTID RGGSDNCDVE SIPEQELCFA