(data stored in ACNUC7421 zone)

SWISSPROT: ALLA_ECO57

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   05-JUL-2017, entry version 92.
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.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., 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.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and 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.,
RA   Cygler M.;
RT   "Crystal structure of ureidoglycolate hydrolase (AllA) from
RT   Escherichia 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
CC       nitrogen source. Reinforces the induction of genes involved in the
CC       degradation of allantoin and glyoxylate by producing glyoxylate.
CC       {ECO:0000255|HAMAP-Rule:MF_00616}.
CC   -!- CATALYTIC ACTIVITY: (S)-ureidoglycolate = glyoxylate + urea.
CC       {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}.
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_MWVM01000032.1.
DR   PDB; 1YQC; X-ray; 1.71 A; A/B=1-160.
DR   PDBsum; 1YQC; -.
DR   ProteinModelPortal; P63486; -.
DR   SMR; P63486; -.
DR   STRING; 155864.Z0659; -.
DR   EnsemblBacteria; AAG54861; AAG54861; Z0659.
DR   EnsemblBacteria; BAB33989; BAB33989; BAB33989.
DR   GeneID; 915530; -.
DR   KEGG; ece:Z0659; -.
DR   KEGG; ecs:ECs0566; -.
DR   PATRIC; fig|386585.9.peg.674; -.
DR   eggNOG; ENOG4108Z2U; Bacteria.
DR   eggNOG; COG3194; LUCA.
DR   HOGENOM; HOG000256169; -.
DR   KO; K01483; -.
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-EC.
DR   GO; GO:0000256; P:allantoin catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.480; -; 1.
DR   HAMAP; MF_00616; Ureidogly_lyase; 1.
DR   InterPro; IPR011051; RmlC_Cupin.
DR   InterPro; IPR007247; Ureidogly_lyase.
DR   InterPro; IPR023525; Ureidogly_lyase_bac.
DR   InterPro; IPR024060; Ureidoglycolate_lyase_dom.
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;
DR   PRODOM; P63486.
DR   SWISS-2DPAGE; P63486.
KW   3D-structure; Complete proteome; Lyase; Purine metabolism.
FT   CHAIN         1    160       Ureidoglycolate lyase.
FT                                /FTId=PRO_0000120549.
FT   STRAND        2      7       {ECO:0000244|PDB:1YQC}.
FT   HELIX        10     13       {ECO:0000244|PDB:1YQC}.
FT   TURN         14     16       {ECO:0000244|PDB:1YQC}.
FT   STRAND       17     20       {ECO:0000244|PDB:1YQC}.
FT   STRAND       27     30       {ECO:0000244|PDB:1YQC}.
FT   TURN         31     34       {ECO:0000244|PDB:1YQC}.
FT   STRAND       35     43       {ECO:0000244|PDB:1YQC}.
FT   STRAND       46     48       {ECO:0000244|PDB:1YQC}.
FT   HELIX        49     51       {ECO:0000244|PDB:1YQC}.
FT   STRAND       53     59       {ECO:0000244|PDB:1YQC}.
FT   STRAND       67     73       {ECO:0000244|PDB:1YQC}.
FT   STRAND       79     86       {ECO:0000244|PDB:1YQC}.
FT   STRAND       90     94       {ECO:0000244|PDB:1YQC}.
FT   STRAND       97     99       {ECO:0000244|PDB:1YQC}.
FT   STRAND      106    109       {ECO:0000244|PDB:1YQC}.
FT   STRAND      115    118       {ECO:0000244|PDB:1YQC}.
FT   STRAND      129    132       {ECO:0000244|PDB:1YQC}.
FT   STRAND      134    140       {ECO:0000244|PDB:1YQC}.
FT   STRAND      148    158       {ECO:0000244|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
//

If you have problems or comments...

PBIL Back to PBIL home page