ID   ALLB_SALDC              Reviewed;         453 AA.
AC   B5FLN3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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}; OrderedLocusNames=SeD_A0571;
OS   Salmonella dublin (strain CT_02021853).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439851;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT_02021853;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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;
CC         Evidence={ECO:0000255|HAMAP-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}.
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DR   EMBL; CP001144; ACH74684.1; -; Genomic_DNA.
DR   RefSeq; WP_000006865.1; NC_011205.1.
DR   AlphaFoldDB; B5FLN3; -.
DR   SMR; B5FLN3; -.
DR   KEGG; sed:SeD_A0571; -.
DR   HOGENOM; CLU_015572_4_2_6; -.
DR   OMA; RNFVCSP; -.
DR   UniPathway; UPA00395; UER00653.
DR   Proteomes; UP000008322; 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   HAMAP; MF_01645; Hydantoinase; 1.
DR   InterPro; IPR017593; Allantoinase.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR03178; allantoinase; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Purine metabolism; Zinc.
FT   CHAIN           1..453
FT                   /note="Allantoinase"
FT                   /id="PRO_1000186927"
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