ALN1_DICDI
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 03-AUG-2022, entry version 99.
DE RecName: Full=Probable allantoinase 1;
DE EC=3.5.2.5;
GN Name=allB1; ORFNames=DDB_G0282199;
OS Dictyostelium discoideum (Slime mold).
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}.
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DR EMBL; AAFI02000046; EAL66305.1; -; Genomic_DNA.
DR RefSeq; XP_640282.1; XM_635190.1.
DR AlphaFoldDB; Q54SV3; -.
DR SMR; Q54SV3; -.
DR STRING; 44689.DDB0231352; -.
DR PaxDb; Q54SV3; -.
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; 1.10.3330.10; -; 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 InterPro; IPR018020; OHCU_decarboxylase.
DR InterPro; IPR036778; OHCU_decarboxylase_sf.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF09349; OHCU_decarbox; 1.
DR SUPFAM; SSF158694; SSF158694; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR03178; allantoinase; 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
