ID   ALLA_BURMA              Reviewed;         170 AA.
AC   Q62JH1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
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}; OrderedLocusNames=BMA1504;
OS   Burkholderia mallei (strain ATCC 23344).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=243160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23344;
RX   PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA   Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA   Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA   Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA   Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA   Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA   Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT   "Structural flexibility in the Burkholderia mallei genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
CC   -!- FUNCTION: Catalyzes the catabolism of the allantoin degradation
CC       intermediate (S)-ureidoglycolate, generating urea and glyoxylate.
CC       Involved in the utilization of allantoin as nitrogen source.
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   -!- SIMILARITY: Belongs to the ureidoglycolate lyase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00616}.
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DR   EMBL; CP000010; AAU47712.1; -; Genomic_DNA.
DR   RefSeq; WP_004193471.1; NC_006348.1.
DR   RefSeq; YP_103148.1; NC_006348.1.
DR   AlphaFoldDB; Q62JH1; -.
DR   SMR; Q62JH1; -.
DR   STRING; 243160.BMA1504; -.
DR   EnsemblBacteria; AAU47712; AAU47712; BMA1504.
DR   GeneID; 56595899; -.
DR   KEGG; bma:BMA1504; -.
DR   PATRIC; fig|243160.12.peg.1549; -.
DR   eggNOG; COG3194; Bacteria.
DR   HOGENOM; CLU_070848_1_0_4; -.
DR   OMA; PLNDKPY; -.
DR   UniPathway; UPA00395; -.
DR   Proteomes; UP000006693; Chromosome 1.
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;
KW   Lyase; Purine metabolism.
FT   CHAIN           1..170
FT                   /note="Ureidoglycolate lyase"
FT                   /id="PRO_1000061349"
SQ   SEQUENCE   170 AA;  18497 MW;  6BFD9B4F1C620573 CRC64;
     MKTLSIEPLT RAAFAPFGDV IETQGAKQIP INLGTTMRFH DLAKIDVADE GGRPLVNLFR
     GQPRTLPFEV TMLERHPLGS QAFVPLTDRP YIVVVAPAGD LDASKIRAFV TSGWQGVNYA
     KGVWHHPLIA LGEVSDFIVV DRGGDGRNLN EQNLPESLWL TDDALLAVGA