ID   A3LNF2_PICST            Unreviewed;       579 AA.
AC   A3LNF2;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 2.
DT   02-SEP-2026, entry version 98.
DE   SubName: Full=Allantoinase {ECO:0000313|EMBL:ABN64845.2};
GN   Name=ALN1 {ECO:0000313|EMBL:ABN64845.2};
GN   ORFNames=PICST_34891 {ECO:0000313|EMBL:ABN64845.2};
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC   Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN64845.2, ECO:0000313|Proteomes:UP000002258};
RN   [1] {ECO:0000313|EMBL:ABN64845.2, ECO:0000313|Proteomes:UP000002258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC   {ECO:0000313|Proteomes:UP000002258};
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; CP000496; ABN64845.2; -; Genomic_DNA.
DR   RefSeq; XP_001382874.2; XM_001382837.1.
DR   AlphaFoldDB; A3LNF2; -.
DR   FunCoup; A3LNF2; 1258.
DR   STRING; 322104.A3LNF2; -.
DR   GeneID; 4836964; -.
DR   KEGG; pic:PICST_34891; -.
DR   eggNOG; KOG2584; Eukaryota.
DR   HOGENOM; CLU_015572_4_0_1; -.
DR   InParanoid; A3LNF2; -.
DR   OMA; SRLHVCH; -.
DR   OrthoDB; 10258955at2759; -.
DR   Proteomes; UP000002258; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0004038; F:allantoinase activity; IEA:TreeGrafter.
DR   GO; GO:0006145; P:purine nucleobase catabolic process; IEA:TreeGrafter.
DR   FunFam; 3.20.20.140:FF:000209; Allantoinase; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR050138; DHOase/Allantoinase_Hydrolase.
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   PANTHER; PTHR43668; ALLANTOINASE; 1.
DR   PANTHER; PTHR43668:SF2; ALLANTOINASE; 1.
DR   Pfam; PF01979; Amidohydro_1; 2.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR   PROSITE; PS01137; TATD_1; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002258}.
FT   DOMAIN          63..196
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   DOMAIN          359..557
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   579 AA;  63080 MW;  42C07E46ECB31004 CRC64;
     MSRAISSTQV LIGTEVVPGT VIFSIESGKI LYIESGKQLE VDDPLLELYN VLPVDHRDVS
     PLVVMPGLVD AHVHLNEPGR TEWEGFATGT KAAAAGGVTT VIDMPLNAIP PTTTIANFNL
     KIDAAKDQTW VDVGFWGGLV PDNLHHLRPL ISMGVRGFKG FMIESGVDEF PAIDPSYIVK
     AMERVEGQKT VLMFHAEMQP VEPLSGDIES ISLGMSASFI QRAPKPVVEL LSMDGSGNCQ
     EEHENCHLPH NHAGSIDHKV LSDAQATALA KSPILAAVEP TFGKFARKAN HFDSPFFRAV
     EEKPLDSPLL IAQSEDALLE DIDPTAYASF LASRPDNFET TAIAEIINCS TKFPTVPLHI
     VHLATHEAVP LIRAAKAKGL PITAETCFHY LSLYAESIAN CSTHFKCCPP IRTNDNRKLL
     WRALRNDIIT TVVSDHSPCT PDLKGLEKGD FFEAWGGISS VGFGLPILYT EGKKLSPPIT
     FAEINKWCSL NTAKQVGLSH RKGKLAVGYD ADLLVFDPND KYIVQNQDTY FKNKLTAYAG
     KEFSGRVIET IVGGNSVYAF GKGHSDVPMG KLILEPRFA
//