ALN2_DICDI
ID ALN2_DICDI Reviewed; 510 AA.
AC Q55C91;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Probable allantoinase 2;
DE EC=3.5.2.5;
GN Name=allB2; ORFNames=DDB_G0270162;
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; AAFI02000005; EAL72431.1; -; Genomic_DNA.
DR RefSeq; XP_646590.1; XM_641498.1.
DR AlphaFoldDB; Q55C91; -.
DR SMR; Q55C91; -.
DR STRING; 44689.DDB0231351; -.
DR PaxDb; Q55C91; -.
DR PRIDE; Q55C91; -.
DR EnsemblProtists; EAL72431; EAL72431; DDB_G0270162.
DR GeneID; 8617561; -.
DR KEGG; ddi:DDB_G0270162; -.
DR dictyBase; DDB_G0270162; allB2.
DR eggNOG; KOG2584; Eukaryota.
DR HOGENOM; CLU_015572_4_0_1; -.
DR InParanoid; Q55C91; -.
DR OMA; WVTAEVT; -.
DR PhylomeDB; Q55C91; -.
DR UniPathway; UPA00395; UER00653.
DR PRO; PR:Q55C91; -.
DR Proteomes; UP000002195; Chromosome 1.
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 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 3: Inferred from homology;
KW Hydrolase; Metal-binding; Purine metabolism; Reference proteome; Zinc.
FT CHAIN 1..510
FT /note="Probable allantoinase 2"
FT /id="PRO_0000330751"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 185
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 185
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 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 185
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 510 AA; 57323 MW; AEA0E212B455B617 CRC64;
MEIWKVIFSI WFLLFQNFVL SAKNDDNKLK VIRGRNVIYN GNVIPLSILI RNGKTIGIKD
YSFNPKKLNE NYEILYDDRE CNNNEDFIIM GGLVDSHVHV NEPGRTEWEG FESATSAAAA
GGVTTIVDMP LNSSPVTTSF KNLLDKIESM KGKLRVDVGL LGGIVPGNSK EIKKMVLQGG
VLGFKSFLLP SGIDEFPPVN ENDIQEAMNE MKLLKCQYNN SDVIMMFHAE VEEPIKEATV
RLKNENADPK LYKTYLDSRP KISENQAISK LIDITRQNQI VSTHIVHLSS SESIEQIREA
MDQGVPISAE TTYNYLHLTS ESVPYGNTLF KSAPPVREHE NKELLWNAII NGTIKLIVSD
HSPCTINLKQ LKEDNQSIGD FLKAWGGISS LELGLPIIWT ECKNRGIPIT QLSEWLSNGP
SKLVGLNDRK GSIEIGRDAD FVIFNPNESF IVNEKKLFLK NKFSAYNGEK LFGVVYETIL
RGNSIFKKGD NKIKKIIGQR LIKSNLINKK
