ID ALLB_RUBXD Reviewed; 454 AA. AC Q1AS71; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 1. DT 05-FEB-2025, entry version 111. 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=Rxyl_2845; OS Rubrobacter xylanophilus (strain DSM 9941 / JCM 11954 / NBRC 16129 / OS PRD-1). OC Bacteria; Bacillati; Actinomycetota; Rubrobacteria; Rubrobacterales; OC Rubrobacteraceae; Rubrobacter. OX NCBI_TaxID=266117; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 9941 / JCM 11954 / NBRC 16129 / PRD-1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S., RA Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.; RT "Complete sequence of Rubrobacter xylanophilus DSM 9941."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000386; ABG05757.1; -; Genomic_DNA. DR RefSeq; WP_011565766.1; NC_008148.1. DR AlphaFoldDB; Q1AS71; -. DR SMR; Q1AS71; -. DR STRING; 266117.Rxyl_2845; -. DR KEGG; rxy:Rxyl_2845; -. DR eggNOG; COG0044; Bacteria. DR HOGENOM; CLU_015572_4_2_11; -. DR OrthoDB; 9803027at2; -. DR PhylomeDB; Q1AS71; -. DR UniPathway; UPA00395; UER00653. DR Proteomes; UP000006637; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. 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:0006145; P:purine nucleobase catabolic process; IEA:TreeGrafter. DR FunFam; 3.20.20.140:FF:000174; Dihydropyrimidinase-related protein 2; 1. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1. DR HAMAP; MF_01645; Hydantoinase; 1. DR InterPro; IPR017593; Allantoinase. DR InterPro; IPR047604; Allantoinase_bact. DR InterPro; IPR006680; Amidohydro-rel. DR InterPro; IPR050138; DHOase/Allantoinase_Hydrolase. DR InterPro; IPR002195; Dihydroorotase_CS. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR032466; Metal_Hydrolase. DR NCBIfam; TIGR03178; allantoinase; 1. DR NCBIfam; TIGR00857; pyrC_multi; 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; Reference proteome; Zinc. FT CHAIN 1..454 FT /note="Allantoinase" FT /id="PRO_0000317681" FT BINDING 60 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01645" FT BINDING 62 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01645" FT BINDING 147 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 147 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 183 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01645" FT BINDING 239 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01645" FT BINDING 312 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 147 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01645" SQ SEQUENCE 454 AA; 48161 MW; 49772AD22B3E7307 CRC64; MSAFDLIVRG GTVVRGGCEV ADVGVADGVI SAVGPDLEGG AREEIDARGL LVLPGAIDAH VHFNEPGRTR WEGFASGTRA LAAGGTTLCV EMPLNAHPPT TDGESFDLKL AAAKASAHVD FALWGGIVPG RVGRMEELAG RGVAGFKAFM SATGTPDFEA ADDLTLYEGM QEAARLGLPV LVHAENRQIT DALARRATSA LRTTMRDYLA SRPAVAELEA IGRAILLASE AGCSLHIVHV STGRGVALVA AARERGVDVT CETCPHYLLF TDEDAVRIGA AAKCAPPLRP REEVESLWEQ VLAGNVAFVT SDHSPCPPDM KAGEDMFRAW GGISGCQSLL PALLDEGYHG RGLPPERLAE LLSANVARRF GFAGKGGIEE GNDADLALVD PSGEHVLREE DLHYRHPISP YVGRSFRGRV VRTILRGRTV FEGGRVVSGP AGRFVRPQRE KGER //