ALLA_ECOLI
ID ALLA_ECOLI Reviewed; 160 AA.
AC P77731; Q2MBS3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
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};
DE AltName: Full=Ureidoglycolate hydrolase;
GN Name=allA {ECO:0000255|HAMAP-Rule:MF_00616}; Synonyms=glxA2, ybbT;
GN OrderedLocusNames=b0505, JW0493;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K12 / ECL1;
RX PubMed=10601204; DOI=10.1128/jb.181.24.7479-7484.1999;
RA Cusa E., Obradors N., Baldoma L., Badia J., Aguilar J.;
RT "Genetic analysis of a chromosomal region containing genes required for
RT assimilation of allantoin nitrogen and linked glyoxylate metabolism in
RT Escherichia coli.";
RL J. Bacteriol. 181:7479-7484(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP CATALYTIC ACTIVITY, COFACTOR, AND FUNCTION.
RC STRAIN=K12;
RX PubMed=24107613; DOI=10.1093/database/bat071;
RA Percudani R., Carnevali D., Puggioni V.;
RT "Ureidoglycolate hydrolase, amidohydrolase, lyase: how errors in biological
RT databases are incorporated in scientific papers and vice versa.";
RL Database 2013:BAT071-BAT071(2013).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), AND SUBUNIT.
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure of ureidoglycolate hydrolase from E.coli. Northeast
RT structural genomics consortium target Et81.";
RL Submitted (JAN-2005) to the PDB data bank.
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, ECO:0000269|PubMed:10601204,
CC ECO:0000269|PubMed:24107613}.
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 ECO:0000269|PubMed:24107613};
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00616,
CC ECO:0000269|PubMed:24107613};
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|Ref.6}.
CC -!- INDUCTION: By glyoxylate and allantoin under anaerobic conditions and
CC by glyoxylate under aerobic conditions.
CC -!- SIMILARITY: Belongs to the ureidoglycolate lyase family.
CC {ECO:0000255|HAMAP-Rule:MF_00616}.
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DR EMBL; U89024; AAB93846.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40258.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73607.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76283.1; -; Genomic_DNA.
DR PIR; H64781; H64781.
DR RefSeq; NP_415038.1; NC_000913.3.
DR RefSeq; WP_000776377.1; NZ_LN832404.1.
DR PDB; 1XSQ; X-ray; 1.60 A; A/B=1-160.
DR PDBsum; 1XSQ; -.
DR AlphaFoldDB; P77731; -.
DR SMR; P77731; -.
DR BioGRID; 4259861; 14.
DR IntAct; P77731; 4.
DR STRING; 511145.b0505; -.
DR PaxDb; P77731; -.
DR PRIDE; P77731; -.
DR EnsemblBacteria; AAC73607; AAC73607; b0505.
DR EnsemblBacteria; BAE76283; BAE76283; BAE76283.
DR GeneID; 945141; -.
DR KEGG; ecj:JW0493; -.
DR KEGG; eco:b0505; -.
DR PATRIC; fig|1411691.4.peg.1772; -.
DR EchoBASE; EB3381; -.
DR eggNOG; COG3194; Bacteria.
DR HOGENOM; CLU_070848_1_1_6; -.
DR InParanoid; P77731; -.
DR OMA; WNIFRCS; -.
DR PhylomeDB; P77731; -.
DR BioCyc; EcoCyc:G6275-MON; -.
DR BioCyc; MetaCyc:G6275-MON; -.
DR UniPathway; UPA00395; -.
DR EvolutionaryTrace; P77731; -.
DR PRO; PR:P77731; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0004848; F:ureidoglycolate hydrolase activity; IEA:InterPro.
DR GO; GO:0050385; F:ureidoglycolate lyase activity; IDA:EcoCyc.
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_0000120547"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1XSQ"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:1XSQ"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:1XSQ"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:1XSQ"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:1XSQ"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1XSQ"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:1XSQ"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:1XSQ"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:1XSQ"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:1XSQ"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:1XSQ"
FT STRAND 101..109
FT /evidence="ECO:0007829|PDB:1XSQ"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:1XSQ"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:1XSQ"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:1XSQ"
FT STRAND 148..158
FT /evidence="ECO:0007829|PDB:1XSQ"
SQ SEQUENCE 160 AA; 18170 MW; 88FDA2A7D48D6E97 CRC64;
MKLQVLPLSQ EAFSAYGDVI ETQQRDFFHI NNGLVERYHD LALVEILEQD CTLISINRAQ
PANLPLTIHE LERHPLGTQA FIPMKGEVFV VVVALGDDKP DLSTLRAFIT NGEQGVNYHR
NVWHHPLFAW QRVTDFLTID RGGSDNCDVE SIPEQELCFA
