ID   ALLA_YEAST              Reviewed;         195 AA.
AC   P32459; D6VVW3;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   24-JAN-2024, entry version 168.
DE   RecName: Full=Ureidoglycolate lyase;
DE            EC=4.3.2.3;
DE   AltName: Full=Degradation of allantoin protein 3;
DE   AltName: Full=Ureidoglycolatase;
DE   AltName: Full=Ureidoglycolate hydrolase;
GN   Name=DAL3; OrderedLocusNames=YIR032C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1776360; DOI=10.1002/yea.320070705;
RA   Yoo H.S., Cooper T.G.;
RT   "The ureidoglycollate hydrolase (DAL3) gene in Saccharomyces cerevisiae.";
RL   Yeast 7:693-698(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169870;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA   Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA   Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA   Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=5965980; DOI=10.1016/0003-2697(66)90177-1;
RA   Choi K.S., Lee K.W., Roush A.H.;
RT   "The assay of yeast ureidoglycolatase.";
RL   Anal. Biochem. 17:413-422(1966).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX   PubMed=3915539; DOI=10.1128/mcb.5.9.2279-2288.1985;
RA   Yoo H.S., Genbauffe F.S., Cooper T.G.;
RT   "Identification of the ureidoglycolate hydrolase gene in the DAL gene
RT   cluster of Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 5:2279-2288(1985).
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 secondary nitrogen source
CC       when primary sources are limiting. {ECO:0000269|PubMed:3915539}.
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:0000269|PubMed:3915539};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.3. {ECO:0000269|PubMed:5965980};
CC   -!- PATHWAY: Nitrogen metabolism; (S)-allantoin degradation.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- INDUCTION: Subject to nitrogen catabolite repression.
CC       {ECO:0000269|PubMed:3915539}.
CC   -!- SIMILARITY: Belongs to the ureidoglycolate lyase family. {ECO:0000305}.
CC   -!- CAUTION: This enzyme was also named ureidoglycolate hydrolase in the
CC       literature. However, this is the recommended name of another enzyme (EC
CC       3.5.1.116) acting on ureidoglycolate. To make the distinction between
CC       ammonia- or urea-releasing activities from ureidoglycolate, the use of
CC       this ambiguous name is deprecated. {ECO:0000305}.
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DR   EMBL; M64778; AAA73025.1; -; Genomic_DNA.
DR   EMBL; Z38061; CAA86192.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08579.1; -; Genomic_DNA.
DR   PIR; S42022; S42022.
DR   RefSeq; NP_012298.1; NM_001179554.1.
DR   AlphaFoldDB; P32459; -.
DR   SMR; P32459; -.
DR   BioGRID; 35023; 122.
DR   DIP; DIP-1284N; -.
DR   IntAct; P32459; 2.
DR   MINT; P32459; -.
DR   STRING; 4932.YIR032C; -.
DR   MaxQB; P32459; -.
DR   PaxDb; 4932-YIR032C; -.
DR   PeptideAtlas; P32459; -.
DR   EnsemblFungi; YIR032C_mRNA; YIR032C; YIR032C.
DR   GeneID; 854850; -.
DR   KEGG; sce:YIR032C; -.
DR   AGR; SGD:S000001471; -.
DR   SGD; S000001471; DAL3.
DR   VEuPathDB; FungiDB:YIR032C; -.
DR   eggNOG; ENOG502S1JQ; Eukaryota.
DR   HOGENOM; CLU_070848_0_1_1; -.
DR   InParanoid; P32459; -.
DR   OMA; ECYFEPG; -.
DR   OrthoDB; 1383619at2759; -.
DR   BioCyc; MetaCyc:YIR032C-MONOMER; -.
DR   BioCyc; YEAST:YIR032C-MONOMER; -.
DR   BRENDA; 4.3.2.3; 984.
DR   UniPathway; UPA00395; -.
DR   BioGRID-ORCS; 854850; 4 hits in 10 CRISPR screens.
DR   PRO; PR:P32459; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P32459; Protein.
DR   GO; GO:0016020; C:membrane; ISS:SGD.
DR   GO; GO:0004848; F:ureidoglycolate hydrolase activity; IEA:InterPro.
DR   GO; GO:0050385; F:ureidoglycolate lyase activity; IDA:SGD.
DR   GO; GO:0000256; P:allantoin catabolic process; IC:SGD.
DR   GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd20298; cupin_UAH; 1.
DR   Gene3D; 2.60.120.480; Ureidoglycolate hydrolase; 1.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   InterPro; IPR047233; UAH_cupin.
DR   InterPro; IPR007247; Ureidogly_lyase.
DR   InterPro; IPR024060; Ureidoglycolate_lyase_dom_sf.
DR   PANTHER; PTHR21221; UREIDOGLYCOLATE HYDROLASE; 1.
DR   PANTHER; PTHR21221:SF1; UREIDOGLYCOLATE LYASE; 1.
DR   Pfam; PF04115; Ureidogly_lyase; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
PE   1: Evidence at protein level;
KW   Lyase; Purine metabolism; Reference proteome.
FT   CHAIN           1..195
FT                   /note="Ureidoglycolate lyase"
FT                   /id="PRO_0000120562"
SQ   SEQUENCE   195 AA;  21727 MW;  6230AEE69585206B CRC64;
     MVTVVAETLT KESFEEYGTI ISPDEEISRM QNLEKGANQG TAIKLLQVSQ VENKSTSKVP
     NWNLFRCFPQ PHLNRVFTQG SNQAISHSIK VLEKHPCSTQ TFVPMGRTSA EVAYLVVVAK
     EIGNKPDLST LRAFTCLGNQ AVTYGLGTWH APMIVLGKEE HLDFSVLIYE SLDPDRPEKD
     CVEEHYSDGD VCIII
//