ID ALLB_SALPK Reviewed; 453 AA. AC B5BD11; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 1. DT 27-MAR-2024, entry version 76. DE RecName: Full=Allantoinase {ECO:0000255|HAMAP-Rule:MF_01645}; DE EC=3.5.2.5 {ECO:0000255|HAMAP-Rule:MF_01645}; DE AltName: Full=Allantoin-utilizing enzyme {ECO:0000255|HAMAP-Rule:MF_01645}; GN Name=allB {ECO:0000255|HAMAP-Rule:MF_01645}; GN OrderedLocusNames=SSPA2045; OS Salmonella paratyphi A (strain AKU_12601). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=554290; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AKU_12601; RX PubMed=19159446; DOI=10.1186/1471-2164-10-36; RA Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A., RA Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N., RA Mungall K., Dougan G., Parkhill J.; RT "Pseudogene accumulation in the evolutionary histories of Salmonella RT enterica serovars Paratyphi A and Typhi."; RL BMC Genomics 10:36-36(2009). CC -!- FUNCTION: Catalyzes the conversion of allantoin (5-ureidohydantoin) to CC allantoic acid by hydrolytic cleavage of the five-member hydantoin CC ring. {ECO:0000255|HAMAP-Rule:MF_01645}. 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01645}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01645}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01645}; CC -!- PATHWAY: Nitrogen metabolism; (S)-allantoin degradation; allantoate CC from (S)-allantoin: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01645}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01645}. CC -!- PTM: Carboxylation allows a single lysine to coordinate two zinc ions. CC {ECO:0000255|HAMAP-Rule:MF_01645}. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC Allantoinase family. {ECO:0000255|HAMAP-Rule:MF_01645}. 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; FM200053; CAR60253.1; -; Genomic_DNA. DR RefSeq; WP_000006865.1; NC_011147.1. DR AlphaFoldDB; B5BD11; -. DR SMR; B5BD11; -. DR KEGG; sek:SSPA2045; -. DR HOGENOM; CLU_015572_4_2_6; -. DR UniPathway; UPA00395; UER00653. DR Proteomes; UP000001869; Chromosome. DR GO; GO:0004038; F:allantoinase activity; IEA:UniProtKB-UniRule. 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-UniRule. DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW. DR CDD; cd01315; L-HYD_ALN; 1. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR HAMAP; MF_01645; Hydantoinase; 1. DR InterPro; IPR017593; Allantoinase. DR InterPro; IPR047604; Allantoinase_bact. DR InterPro; IPR006680; Amidohydro-rel. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR032466; Metal_Hydrolase. DR NCBIfam; TIGR03178; allantoinase; 1. DR PANTHER; PTHR43668; ALLANTOINASE; 1. DR PANTHER; PTHR43668:SF4; ALLANTOINASE; 1. DR Pfam; PF01979; Amidohydro_1; 1. DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1. PE 3: Inferred from homology; KW Hydrolase; Metal-binding; Purine metabolism; Zinc. FT CHAIN 1..453 FT /note="Allantoinase" FT /id="PRO_1000186932" FT BINDING 59 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01645" FT BINDING 61 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01645" FT BINDING 146 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /note="via carbamate group" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01645" FT BINDING 146 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /note="via carbamate group" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01645" FT BINDING 186 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01645" FT BINDING 242 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01645" FT BINDING 315 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01645" FT MOD_RES 146 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01645" SQ SEQUENCE 453 AA; 49887 MW; 223BFADF6257891E CRC64; MSFDLIIKNG TVILENEARV IDIAVQGGKI AAIGENLGEA KNVLDATGLI VSPGMVDAHT HISEPGRTHW EGYETGTRAA AKGGITTMIE MPLNQLPATV DRETIELKFD AAKGKLTIDA AQLGGLVSYN LDRLHELDEV GVVGFKCFVA TCGDRGIDND FRDVNDWQFY KGAQKLGEMD QTVLVHCENA LICDELGEEA KREGRVTAHD YVASRPVFTE VEAIRRVLYL AKAAGCRLHV CHISSPEGVE EVTRARQEGQ DVTCESCPHY FVLDTDQFEE IGTLAKCSPP IRDQENQKGM WEKLFNGEID CLVSDHSPCP PEMKAGNIMQ AWGGIAGLQN CMDVMFDEAV QKRGMSLPMF GKLMATNAAD IFGLKHKGRI APGKDADLVF IQPDSSYVLK NEDLEYRHKV SPYVGRTIGA RITKTILRGD VIYDIEHGFP VPPKGQFILK HQQ //