ID   ALN_LITCT               Reviewed;         484 AA.
AC   P40757;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Allantoinase, mitochondrial;
DE            EC=3.5.2.5;
DE   Flags: Precursor;
GN   Name=ALN;
OS   Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX   NCBI_TaxID=8400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 365-381.
RC   TISSUE=Liver;
RX   PubMed=8163532; DOI=10.1016/s0021-9258(17)32711-4;
RA   Hayashi S., Jain S., Chu R., Alvares K., Xu B., Erfurth F., Usuda N.,
RA   Rao M.S., Reddy S.K., Noguchi T., Reddy J.K., Yeldandi A.Y.;
RT   "Amphibian allantoinase. Molecular cloning, tissue distribution, and
RT   functional expression.";
RL   J. Biol. Chem. 269:12269-12276(1994).
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;
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.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- TISSUE SPECIFICITY: Liver and kidney.
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; U03471; AAA19116.1; -; mRNA.
DR   PIR; A53595; A53595.
DR   AlphaFoldDB; P40757; -.
DR   SMR; P40757; -.
DR   UniPathway; UPA00395; UER00653.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004038; F:allantoinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000256; P:allantoin catabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR017593; Allantoinase.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR002195; Dihydroorotase_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   Direct protein sequencing; Hydrolase; Metal-binding; Mitochondrion;
KW   Transit peptide; Zinc.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..484
FT                   /note="Allantoinase, mitochondrial"
FT                   /id="PRO_0000007371"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
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         163
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         199
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         251
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         324
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         163
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   484 AA;  53257 MW;  A2DC377B850DC402 CRC64;
     MALKSKPGIM NITPGSKISV IRSKRVIQAN TISSCDIIIS DGKISSVLAW GKHVTSGAKL
     LDVGDLVVMA GIIDPHVHVN EPGRTDWEGY RTATLAAAAG GITAIVDMPL NSLPPTTSVT
     NFHTKLQAAK RQCYVDVAFW GGVIPDNQVE LIPMLQAGVA GFKCFLINSG VPEFPHVSVT
     DLHTAMSELQ GTNSVLLFHA ELEIAKPAPE IGDSTLYQTF LDSRPDDMEI AAVQLVADLC
     QQYKVRCHIV HLSSAQSLTI IRKAKEAGAP LTVETTHHYL SLSSEHIPPG ATYFKCCPPV
     RGHRNKEALW NALLQGHIDM VVSDHSPCTP DLKLLKEGDY MKAWGGISSL QFGLPLFWTS
     ARTRGFSLTD VSQLLSSNTA KLCGLGIVKE PLKWVMMLIW SSGILTKSFR CKKMIFITRI
     SSPHIWDSFF KEKSWLLLFE GLLFISKGSM LPNQLENLFL YTLWSLVKPV HPVHPIIRKN
     LPHI