ALLC_YEAST
ID ALLC_YEAST Reviewed; 343 AA.
AC P25335; D6VVW0;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Allantoicase;
DE EC=3.5.3.4;
DE AltName: Full=Allantoate amidinohydrolase;
GN Name=DAL2; Synonyms=ALC1; OrderedLocusNames=YIR029W;
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=1916277; DOI=10.1016/0378-1119(91)90464-m;
RA Yoo H.S., Cooper T.G.;
RT "Sequences of two adjacent genes, one (DAL2) encoding allantoicase and
RT another (DCG1) sensitive to nitrogen-catabolite repression in Saccharomyces
RT cerevisiae.";
RL Gene 104:55-62(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1839481; DOI=10.1002/yea.320070912;
RA Lee F.-J.S., Moss J.;
RT "Cloning of a Saccharomyces cerevisiae gene encoding a protein homologous
RT to allantoicase of Neurospora crassa.";
RL Yeast 7:993-995(1991).
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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=15020593; DOI=10.1074/jbc.m401336200;
RA Leulliot N., Quevillon-Cheruel S., Sorel I., Graille M., Meyer P.,
RA Liger D., Blondeau K., Janin J., van Tilbeurgh H.;
RT "Crystal structure of yeast allantoicase reveals a repeated jelly roll
RT motif.";
RL J. Biol. Chem. 279:23447-23452(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=15229895; DOI=10.1002/prot.20164;
RA Xu Q., Schwarzenbacher R., Page R., Sims E., Abdubek P., Ambing E.,
RA Biorac T., Brinen L.S., Cambell J., Canaves J.M., Chiu H.J., Dai X.,
RA Deacon A.M., DiDonato M., Elsliger M.-A., Floyd R., Godzik A., Grittini C.,
RA Grzechnik S.K., Hampton E., Jaroszewski L., Karlak C., Klock H.E.,
RA Koesema E., Kovarik J.S., Kreusch A., Kuhn P., Lesley S.A., Levin I.,
RA McMullan D., McPhillips T.M., Miller M.D., Morse A., Moy K., Ouyang J.,
RA Quijano K., Reyes R., Rezezadeh F., Robb A., Spraggon G., Stevens R.C.,
RA van den Bedem H., Velasquez J., Vincent J., von Delft F., Wang X., West B.,
RA Wolf G., Hodgson K.O., Wooley J., Wilson I.A.;
RT "Crystal structure of an allantoicase (YIR029W) from Saccharomyces
RT cerevisiae at 2.4 A resolution.";
RL Proteins 56:619-624(2004).
CC -!- FUNCTION: Utilization of purines as secondary nitrogen sources, when
CC primary sources are limiting.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=allantoate + H2O = (S)-ureidoglycolate + urea;
CC Xref=Rhea:RHEA:11016, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199,
CC ChEBI:CHEBI:17536, ChEBI:CHEBI:57296; EC=3.5.3.4;
CC -!- PATHWAY: Nitrogen metabolism; (S)-allantoin degradation; (S)-
CC ureidoglycolate from allantoate (aminidohydrolase route): step 1/1.
CC -!- INDUCTION: Repressed by nitrogen.
CC -!- SIMILARITY: Belongs to the allantoicase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M64720; AAA34554.1; -; Genomic_DNA.
DR EMBL; X60460; CAA42994.1; -; Genomic_DNA.
DR EMBL; Z38061; CAA86189.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08576.1; -; Genomic_DNA.
DR PIR; JH0442; JH0442.
DR RefSeq; NP_012295.1; NM_001179551.1.
DR PDB; 1O59; X-ray; 2.40 A; A=1-343.
DR PDB; 1SG3; X-ray; 2.60 A; A/B=1-343.
DR PDBsum; 1O59; -.
DR PDBsum; 1SG3; -.
DR AlphaFoldDB; P25335; -.
DR SMR; P25335; -.
DR BioGRID; 35020; 97.
DR IntAct; P25335; 1.
DR STRING; 4932.YIR029W; -.
DR MaxQB; P25335; -.
DR PaxDb; P25335; -.
DR PRIDE; P25335; -.
DR EnsemblFungi; YIR029W_mRNA; YIR029W; YIR029W.
DR GeneID; 854847; -.
DR KEGG; sce:YIR029W; -.
DR SGD; S000001468; DAL2.
DR VEuPathDB; FungiDB:YIR029W; -.
DR eggNOG; KOG4145; Eukaryota.
DR GeneTree; ENSGT00390000001793; -.
DR HOGENOM; CLU_038797_0_0_1; -.
DR InParanoid; P25335; -.
DR OMA; MDDGWET; -.
DR BioCyc; MetaCyc:YIR029W-MON; -.
DR BioCyc; YEAST:YIR029W-MON; -.
DR UniPathway; UPA00395; UER00654.
DR EvolutionaryTrace; P25335; -.
DR PRO; PR:P25335; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P25335; protein.
DR GO; GO:0004037; F:allantoicase activity; IDA:SGD.
DR GO; GO:0000256; P:allantoin catabolic process; IMP:SGD.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR HAMAP; MF_00813; Allantoicase; 1.
DR InterPro; IPR005164; Allantoicase.
DR InterPro; IPR015908; Allantoicase_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR PANTHER; PTHR12045; PTHR12045; 1.
DR Pfam; PF03561; Allantoicase; 2.
DR PIRSF; PIRSF016516; Allantoicase; 1.
DR SUPFAM; SSF49785; SSF49785; 2.
DR TIGRFAMs; TIGR02961; allantoicase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Purine metabolism; Reference proteome.
FT CHAIN 1..343
FT /note="Allantoicase"
FT /id="PRO_0000205914"
FT CONFLICT 93
FT /note="A -> S (in Ref. 2; CAA42994)"
FT /evidence="ECO:0000305"
FT CONFLICT 134..135
FT /note="WV -> SL (in Ref. 2; CAA42994)"
FT /evidence="ECO:0000305"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:1O59"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:1O59"
FT HELIX 9..16
FT /evidence="ECO:0007829|PDB:1O59"
FT TURN 17..20
FT /evidence="ECO:0007829|PDB:1O59"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:1O59"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:1O59"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1O59"
FT HELIX 45..49
FT /evidence="ECO:0007829|PDB:1O59"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1O59"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1O59"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:1O59"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:1O59"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:1O59"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:1O59"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:1O59"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:1O59"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:1O59"
FT STRAND 162..171
FT /evidence="ECO:0007829|PDB:1O59"
FT STRAND 174..184
FT /evidence="ECO:0007829|PDB:1O59"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1O59"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:1O59"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:1O59"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:1O59"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:1O59"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:1O59"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:1O59"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:1O59"
FT STRAND 257..265
FT /evidence="ECO:0007829|PDB:1O59"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:1O59"
FT STRAND 275..282
FT /evidence="ECO:0007829|PDB:1O59"
FT STRAND 297..305
FT /evidence="ECO:0007829|PDB:1O59"
FT STRAND 311..319
FT /evidence="ECO:0007829|PDB:1O59"
FT STRAND 323..331
FT /evidence="ECO:0007829|PDB:1O59"
FT STRAND 337..343
FT /evidence="ECO:0007829|PDB:1O59"
SQ SEQUENCE 343 AA; 38714 MW; 0F9CB0FBA5EB76F1 CRC64;
MKFFSLADEA EFKSIIISKN KAVDVIGSKL GGQVVSFSDE WFASAENLIQ PTAPIRDPTR
FVHSGAWYDG WETRRHNEME YDWVIIKMGV AAAHIIGGEI DTAFFNGNHA PFVSIEALYD
EGEEGNIVED DSRWVEIVEK FECGPSQRHL FVRGNGLTKE RFTHIKLKMY PDGGIARFRL
YGRVVPPELK TKDHIIDLAY VCNGAVALKY SDQHFGSVDN LLLPGRGHDM SDGWETKRSR
QPGHTDWAVI QLGRESSFIE KIIVDTAHFR GNFPQFITVE GCLKESESSE NTGEGTWVEL
VGKSKTGPDK EHVYEIRKSI RVSHVKLTII PDGGVKRIRV WGY
