ALLA_SHIFL
ID ALLA_SHIFL Reviewed; 160 AA.
AC P63487; Q8XCX8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 121.
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=SF0444, S0451;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND SUBUNIT.
RG Northeast structural genomics consortium (NESG);
RT "X-ray structure of Northeast structural genomics consortium target Sfr7.";
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}.
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|Ref.3}.
CC -!- SIMILARITY: Belongs to the ureidoglycolate lyase family.
CC {ECO:0000255|HAMAP-Rule:MF_00616}.
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DR EMBL; AE005674; AAN42098.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP15974.1; -; Genomic_DNA.
DR RefSeq; NP_706391.1; NC_004337.2.
DR RefSeq; WP_000776388.1; NZ_WHSI01000019.1.
DR PDB; 1XSR; X-ray; 2.80 A; A/B=1-160.
DR PDBsum; 1XSR; -.
DR AlphaFoldDB; P63487; -.
DR SMR; P63487; -.
DR STRING; 198214.SF0444; -.
DR EnsemblBacteria; AAN42098; AAN42098; SF0444.
DR EnsemblBacteria; AAP15974; AAP15974; S0451.
DR GeneID; 1027733; -.
DR GeneID; 58462776; -.
DR KEGG; sfl:SF0444; -.
DR KEGG; sfx:S0451; -.
DR PATRIC; fig|198214.7.peg.509; -.
DR HOGENOM; CLU_070848_1_1_6; -.
DR OMA; WNIFRCS; -.
DR OrthoDB; 1597997at2; -.
DR UniPathway; UPA00395; -.
DR EvolutionaryTrace; P63487; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000120559"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1XSR"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:1XSR"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:1XSR"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:1XSR"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1XSR"
FT TURN 31..34
FT /evidence="ECO:0007829|PDB:1XSR"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:1XSR"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1XSR"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:1XSR"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:1XSR"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:1XSR"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:1XSR"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:1XSR"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1XSR"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:1XSR"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:1XSR"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:1XSR"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:1XSR"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:1XSR"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:1XSR"
SQ SEQUENCE 160 AA; 18223 MW; E39014610FE93FC6 CRC64;
MKLQVLPLSQ EAFSAYGDVI ETQQRDFFHI NNGLVERYHD LALVEILEQD RTLISINRAQ
PANLPLTIHE LERHPLGTQA FIPMKGEVFV VVVALGDDKP DLSTLRAFIT NGEQGVNYHR
NVWHHPLFAW QRVTDFLTID RGGSDNCDVE SIPEQELCFA
