ALN_YEAST
ID ALN_YEAST Reviewed; 460 AA.
AC P32375; D6VVV8;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Allantoinase;
DE EC=3.5.2.5 {ECO:0000305|PubMed:1803816};
GN Name=DAL1; OrderedLocusNames=YIR027C;
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], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=1803816; DOI=10.1002/yea.320070903;
RA Buckholz R.G., Cooper T.G.;
RT "The allantoinase (DAL1) gene of Saccharomyces cerevisiae.";
RL Yeast 7:913-923(1991).
RN [2]
RP ERRATUM OF PUBMED:1803816.
RA Buckholz R.G., Cooper T.G.;
RL Yeast 8:239-239(1992).
RN [3]
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 [4]
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).
CC -!- FUNCTION: Catalyzes the conversion of allantoin (5-ureidohydantoin) to
CC allantoic acid by hydrolytic cleavage of the five-member hydantoin
CC ring. Involved in the utilization of purines as secondary nitrogen
CC sources, when primary sources are limiting.
CC {ECO:0000305|PubMed:1803816}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-allantoin + H2O = allantoate + H(+); Xref=Rhea:RHEA:17029,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15678,
CC ChEBI:CHEBI:17536; EC=3.5.2.5; Evidence={ECO:0000305|PubMed:1803816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17030;
CC Evidence={ECO:0000305|PubMed:1803816};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Nitrogen metabolism; (S)-allantoin degradation; allantoate
CC from (S)-allantoin: step 1/1. {ECO:0000305|PubMed:1803816}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- PTM: Carboxylation allows a single lysine to coordinate two zinc ions.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Allantoinase family. {ECO:0000305}.
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DR EMBL; M69294; AAA34553.1; -; Genomic_DNA.
DR EMBL; Z38061; CAA86187.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08574.1; -; Genomic_DNA.
DR PIR; S48489; S48489.
DR RefSeq; NP_012293.3; NM_001179549.3.
DR AlphaFoldDB; P32375; -.
DR SMR; P32375; -.
DR BioGRID; 35018; 60.
DR DIP; DIP-4280N; -.
DR STRING; 4932.YIR027C; -.
DR PaxDb; P32375; -.
DR EnsemblFungi; YIR027C_mRNA; YIR027C; YIR027C.
DR GeneID; 854845; -.
DR KEGG; sce:YIR027C; -.
DR SGD; S000001466; DAL1.
DR VEuPathDB; FungiDB:YIR027C; -.
DR eggNOG; KOG2584; Eukaryota.
DR GeneTree; ENSGT01030000234527; -.
DR HOGENOM; CLU_015572_4_0_1; -.
DR InParanoid; P32375; -.
DR OMA; QHAQEPR; -.
DR BioCyc; MetaCyc:YIR027C-MON; -.
DR BioCyc; YEAST:YIR027C-MON; -.
DR UniPathway; UPA00395; UER00653.
DR PRO; PR:P32375; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P32375; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004038; F:allantoinase activity; IMP:SGD.
DR GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009442; P:allantoin assimilation pathway; IMP:SGD.
DR GO; GO:0006145; P:purine nucleobase catabolic process; IBA:GO_Central.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR017593; Allantoinase.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR002195; Dihydroorotase_CS.
DR InterPro; IPR018228; DNase_TatD-rel_CS.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR03178; allantoinase; 1.
DR PROSITE; PS00482; DIHYDROOROTASE_1; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Purine metabolism; Reference proteome; Zinc.
FT CHAIN 1..460
FT /note="Allantoinase"
FT /id="PRO_0000165939"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 157
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
FT CONFLICT 438..460
FT /note="VVYTNANGVSKTPLGQTLLDSRR -> WYIRMPTESRKHHWVKLCLILDVKL
FT KLQIFIKEIL (in Ref. 1; AAA34553)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 50126 MW; 887480809B6A8F42 CRC64;
MPINAITSDH VIINGANKPA TIVYSTESGT ILDVLEGSVV MEKTEITKYE IHTLENVSPC
TILPGLVDSH VHLNEPGRTS WEGFETGTQA AISGGVTTVV DMPLNAIPPT TNVENFRIKL
EAAEGQMWCD VGFWGGLVPH NLPDLIPLVK AGVRGFKGFL LDSGVEEFPP IGKEYIEEAL
KVLAEEDTMM MFHAELPKAH EDQQQPEQSH REYSSFLSSR PDSFEIDAIN LILECLRARN
GPVPPVHIVH LASMKAIPLI RKARASGLPV TTETCFHYLC IAAEQIPDGA TYFKCCPPIR
SESNRQGLWD ALREGVIGSV VSDHSPCTPE LKNLQKGDFF DSWGGIASVG LGLPLMFTQG
CSLVDIVTWC CKNTSHQVGL SHQKGTIAPG YDADLVVFDT ASKHKISNSS VYFKNKLTAY
NGMTVKGTVL KTILRGQVVY TNANGVSKTP LGQTLLDSRR
