(data stored in SCRATCH zone)

SWISSPROT: C8U2I7_ECO10

ID   C8U2I7_ECO10            Unreviewed;       160 AA.
AC   C8U2I7;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 66.
DE   RecName: Full=Ureidoglycolate lyase {ECO:0000256|HAMAP-Rule:MF_00616, ECO:0000256|SAAS:SAAS00671785};
DE            EC=4.3.2.3 {ECO:0000256|HAMAP-Rule:MF_00616, ECO:0000256|SAAS:SAAS00671785};
DE   AltName: Full=Ureidoglycolatase {ECO:0000256|HAMAP-Rule:MF_00616};
GN   Name=allA {ECO:0000256|HAMAP-Rule:MF_00616,
GN   ECO:0000313|EMBL:BAI29345.1};
GN   OrderedLocusNames=ECO103_0478 {ECO:0000313|EMBL:BAI29345.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29345.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29345.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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
CC       nitrogen source. Reinforces the induction of genes involved in the
CC       degradation of allantoin and glyoxylate by producing glyoxylate.
CC       {ECO:0000256|HAMAP-Rule:MF_00616}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-ureidoglycolate = glyoxylate + urea;
CC         Xref=Rhea:RHEA:11304, ChEBI:CHEBI:16199, ChEBI:CHEBI:36655,
CC         ChEBI:CHEBI:57296; EC=4.3.2.3; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00616, ECO:0000256|SAAS:SAAS01117877};
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00616, ECO:0000256|SAAS:SAAS00343213};
CC   -!- PATHWAY: Nitrogen metabolism; (S)-allantoin degradation.
CC       {ECO:0000256|HAMAP-Rule:MF_00616, ECO:0000256|SAAS:SAAS00671779}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00616,
CC       ECO:0000256|SAAS:SAAS00671777}.
CC   -!- SIMILARITY: Belongs to the ureidoglycolate lyase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00616, ECO:0000256|SAAS:SAAS00671784}.
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DR   EMBL; AP010958; BAI29345.1; -; Genomic_DNA.
DR   RefSeq; WP_000776392.1; NC_013353.1.
DR   SMR; C8U2I7; -.
DR   EnsemblBacteria; BAI29345; BAI29345; ECO103_0478.
DR   KEGG; eoh:ECO103_0478; -.
DR   HOGENOM; HOG000256169; -.
DR   KO; K01483; -.
DR   OMA; ANWNIFR; -.
DR   BioCyc; ECOL585395:ECO103_RS02500-MONOMER; -.
DR   UniPathway; UPA00395; -.
DR   Proteomes; UP000000959; 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;
DR   PRODOM; C8U2I7.
DR   SWISS-2DPAGE; C8U2I7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Hydrolase {ECO:0000313|EMBL:BAI29345.1};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00616,
KW   ECO:0000256|SAAS:SAAS00671778};
KW   Purine metabolism {ECO:0000256|HAMAP-Rule:MF_00616,
KW   ECO:0000256|SAAS:SAAS00671775}.
SQ   SEQUENCE   160 AA;  18249 MW;  F891A4710EF92EC7 CRC64;
     MKLQVLPLSQ EAFSAYGDVI ETQQRDFFHI NNGLVERYHD LALVEILEQD RTLISINRAQ
     PANLPLTIYE LERHPLGTQA FIPMKGEVFV VVVALGDDKP DLSTLRAFIT NGEQGVNYHR
     NVWHHPLFAW QRVTDFLTID RGGSDNCDVE SIPEQELCFA
//

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