ID   ALN1_DICDI              Reviewed;         649 AA.
AC   Q54SV3;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   RecName: Full=Probable allantoinase 1;
DE            EC=3.5.2.5;
GN   Name=allB1; ORFNames=DDB_G0282199;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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   -!- 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}.
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; AAFI02000046; EAL66305.1; -; Genomic_DNA.
DR   RefSeq; XP_640282.1; XM_635190.1.
DR   AlphaFoldDB; Q54SV3; -.
DR   SMR; Q54SV3; -.
DR   STRING; 44689.Q54SV3; -.
DR   PaxDb; 44689-DDB0231352; -.
DR   EnsemblProtists; EAL66305; EAL66305; DDB_G0282199.
DR   GeneID; 8623457; -.
DR   KEGG; ddi:DDB_G0282199; -.
DR   dictyBase; DDB_G0282199; allB1.
DR   eggNOG; KOG2584; Eukaryota.
DR   HOGENOM; CLU_015572_4_0_1; -.
DR   InParanoid; Q54SV3; -.
DR   OMA; HICHVSH; -.
DR   PhylomeDB; Q54SV3; -.
DR   UniPathway; UPA00395; UER00653.
DR   PRO; PR:Q54SV3; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004038; F:allantoinase activity; ISS:dictyBase.
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; ISS:dictyBase.
DR   GO; GO:0006145; P:purine nucleobase catabolic process; IBA:GO_Central.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 1.10.3330.10; Oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase; 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   InterPro; IPR018020; OHCU_decarboxylase.
DR   InterPro; IPR036778; OHCU_decarboxylase_sf.
DR   NCBIfam; TIGR03178; allantoinase; 1.
DR   PANTHER; PTHR43668; ALLANTOINASE; 1.
DR   PANTHER; PTHR43668:SF2; ALLANTOINASE; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF09349; OHCU_decarbox; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF158694; UraD-Like; 1.
DR   PROSITE; PS00482; DIHYDROOROTASE_1; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Purine metabolism; Reference proteome; Zinc.
FT   CHAIN           1..649
FT                   /note="Probable allantoinase 1"
FT                   /id="PRO_0000330750"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
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         154
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         197
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         255
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         329
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         154
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   649 AA;  72476 MW;  1E4C7067D47B28F2 CRC64;
     MNSENIIKVI KGKKVVINGE IKPASILIKN GIIIDIKDYS SEIKEEHEVL IEEEKLVIMG
     GLVDSHVHIN EPGRTEWEGF LSATSAAASG GVTTIIDMPL NSSPVTTTFE NLQTKIESMP
     GKLRVDVGLL GGIIPGNSSE ISRMVLEGGV VGFKSFLVHS GIDEFPHVKE DDIQEAMNVM
     KKLKDEQGGR DVVMMFHAEI EEPIKEATER LQRENADPKL YDTFLKSRPR VSENIAIDKV
     IELTKKNMIK THIVHLSSSD AIEAIHEAVH NDGVPITAET TYHYLYFESE QVPYGNTLYK
     CCPPVRESEN KDLLWKAVTN GTINIIVSDH SPCTLDLKLI EQGDFMKAWG GISSLQLGLP
     IIWTEASKRG VPLAKLSEYM SDAPSRLVGL NDRKGSIKIG RDADFVIWDP EESFTVDQGL
     LMVKNKNSPY HGEKLLGVVH HTILRGNKIF SKGDQTISKI IGKRLIQTKI HTNPIYPSPT
     LPTIELLNSL TEQKTFFDCI HLLFEAAPPL ANALFSKRPF SSYQQLIDQA YSIIQSLNES
     DKIQVINAHP RIGVSASQVK NSSSISYREQ SCDKDSSIDQ SILENLTQLN QQYESKFGFK
     FVVFVNGRPK NEIIPILQNR LNNNDKQKEL NLGLSEMIEI SKSRLLKLL
//