ID ALLB_ECODH Reviewed; 453 AA. AC B1XGB0; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 1. DT 27-MAR-2024, entry version 81. 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=ECDH10B_0468; OS Escherichia coli (strain K12 / DH10B). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=316385; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / DH10B; RX PubMed=18245285; DOI=10.1128/jb.01695-07; RA Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B., RA Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B., RA Posfai G., Weinstock G.M., Blattner F.R.; RT "The complete genome sequence of Escherichia coli DH10B: insights into the RT biology of a laboratory workhorse."; RL J. Bacteriol. 190:2597-2606(2008). 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; CP000948; ACB01637.1; -; Genomic_DNA. DR RefSeq; WP_000006900.1; NC_010473.1. DR AlphaFoldDB; B1XGB0; -. DR SMR; B1XGB0; -. DR KEGG; ecd:ECDH10B_0468; -. DR HOGENOM; CLU_015572_4_2_6; -. DR UniPathway; UPA00395; UER00653. 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 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..453 FT /note="Allantoinase" FT /id="PRO_1000186922" 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; 49602 MW; 5CFE588F94268AB4 CRC64; MSFDLIIKNG TVILENEARV VDIAVKGGKI AAIGQDLGDA KEVMDASGLV VSPGMVDAHT HISEPGRSHW EGYETGTRAA AKGGITTMIE MPLNQLPATV DRASIELKFD AAKGKLTIDA AQLGGLVSYN IDRLHELDEV GVVGFKCFVA TCGDRGIDND FRDVNDWQFF KGAQKLGELG QPVLVHCENA LICDELGEEA KREGRVTAHD YVASRPVFTE VEAIRRVLYL AKVAGCRLHV CHVSSPEGVE EVTRARQEGQ DVTCESCPHY FVLDTDQFEE IGTLAKCSPP IRDLENQKGM WEKLFNGEID CLVSDHSPCP PEMKAGNIMK AWGGIAGLQS CMDVMFDEAV QKRGMSLPMF GKLMATNAAD IFGLQQKGRI APGKDADFVF IQPNSSYVLT NDDLEYRHKV SPYVGRTIGA RITKTILRGD VIYDIEQGFP VAPKGQFILK HQQ //