ID ALLB_BACVZ Reviewed; 454 AA. AC A7Z8F5; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 27-MAR-2024, entry version 101. 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 Synonyms=pucH {ECO:0000255|HAMAP-Rule:MF_01645}; GN OrderedLocusNames=RBAM_029500; OS Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42) OS (Bacillus amyloliquefaciens subsp. plantarum). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus amyloliquefaciens group. OX NCBI_TaxID=326423; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42; RX PubMed=17704766; DOI=10.1038/nbt1325; RA Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., RA Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., RA Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., RA Strittmatter A., Gottschalk G., Borriss R.; RT "Comparative analysis of the complete genome sequence of the plant growth- RT promoting bacterium Bacillus amyloliquefaciens FZB42."; RL Nat. Biotechnol. 25:1007-1014(2007). 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; CP000560; ABS75281.1; -; Genomic_DNA. DR RefSeq; WP_012118360.1; NC_009725.2. DR AlphaFoldDB; A7Z8F5; -. DR SMR; A7Z8F5; -. DR KEGG; bay:RBAM_029500; -. DR HOGENOM; CLU_015572_4_0_9; -. DR UniPathway; UPA00395; UER00653. DR Proteomes; UP000001120; 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 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; 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..454 FT /note="Allantoinase" FT /id="PRO_0000317668" 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; 49454 MW; BCA128C60A38F03C CRC64; MAYDVIVKGA KAVRKGGTER ADIAVKDGKI ALIGPGIDEN AEQVVQADGM YVFPGAVDCH VHFNEPGREE WEGIETGSNM LAAGGCTSYF DMPLNCIPST VTAENLLAKA EIAERKSAVD FALWGGLMPG YTEHIRPMAE AGAIGFKAFL SKSGTDEFQS ADERTLLKGM KEIAACGKVL ALHAESDALT RFLEAEYALQ GKIDVRAYAS SRPEEAECEA VQRAIEYARA TGCALHFVHI STKRAVLSIQ QAKKDGLDVT VETCPHYLLF SFEDFLKKGA AAKCAPPLRS EADKEELIGV LAEGLIDMVS SDHSPCHPSL KREDNMFLSW GGISGGQFTL LGMIQLAIDH GIPFEHVARW TAEAPAKRFG LTNKGRLEEG FDADFAIVRP EPFTVTKETM FSKHKQSLYE GHTFPYRIAA TYSKGRCVYQ DGGRKQSGAF GTFLKPSEIK EPIL //