ID ALLB_ECOLC Reviewed; 453 AA. AC B1IZ89; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 85. 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=EcolC_3111; OS Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / OS WDCM 00012 / Crooks). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=481805; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / RC Crooks; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C., RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Ingram L., Richardson P.; RT "Complete sequence of Escherichia coli C str. ATCC 8739."; RL Submitted (FEB-2008) 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; CP000946; ACA78734.1; -; Genomic_DNA. DR RefSeq; WP_000006890.1; NZ_MTFT01000020.1. DR AlphaFoldDB; B1IZ89; -. DR SMR; B1IZ89; -. DR KEGG; ecl:EcolC_3111; -. 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_1000088216" 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; 49530 MW; C9FFEEA8BD5946FD CRC64; MSFDLIIKNG TVILENEARV VDIAVKGGKI AAIGQDLGDA KEVMDASGLV VSPGMVDAHT HISEPGRSHW EGYETGTRAA AKGGITTMIE MPLNQLPATV DRASIELKFD AAKGKLTIDA AQLGGLVSYN IDRLHELDEV GVVGFKCFVA TCGDRGIDND FRDVNDWQFF KGAQKLGELG QPVLVHCENA LICDALGEEA KSEGRVTAHD YVASRPVFTE VEAIRRVLYL AKVAGCRLHI CHISSPEGVE EVTRARQEGQ DVTCESCPHY FVLDTDQFEE IGTLAKCSPP IRDLENQKGM WEKLFNGEID CLVSDHSPCP PEMKAGNIME AWGGIAGLQN CMDVMFDEAV QKRGMSLPMF GKLMATNAAD IFGLQQKGRI APGKDADFVF IQPNSSYVLT NDDLEYRHKV SPYVGRTIGA RITKTILRGD VIYDIEQGFP VAPKGQFILK HQQ //