ID   ALLB_BACLD              Reviewed;         454 AA.
AC   Q65LN0; Q62X22;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 117.
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=BLi01126, BL01094;
OS   Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS   NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB
RC   9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15383718; DOI=10.1159/000079829;
RA   Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA   Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT   "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT   with great industrial potential.";
RL   J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB
RC   9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA   Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA   Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:R77.1-R77.12(2004).
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}.
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DR   EMBL; CP000002; AAU22686.1; -; Genomic_DNA.
DR   EMBL; AE017333; AAU40034.1; -; Genomic_DNA.
DR   RefSeq; WP_011197731.1; NC_006322.1.
DR   AlphaFoldDB; Q65LN0; -.
DR   SMR; Q65LN0; -.
DR   STRING; 279010.BL01094; -.
DR   GeneID; 66216742; -.
DR   KEGG; bld:BLi01126; -.
DR   KEGG; bli:BL01094; -.
DR   eggNOG; COG0044; Bacteria.
DR   HOGENOM; CLU_015572_4_2_9; -.
DR   BRENDA; 3.5.2.5; 669.
DR   UniPathway; UPA00395; UER00653.
DR   Proteomes; UP000000606; Chromosome.
DR   Bgee; BL01094; Expressed in ovary and 11 other cell types or tissues.
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; Reference proteome; Zinc.
FT   CHAIN           1..454
FT                   /note="Allantoinase"
FT                   /id="PRO_0000317671"
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         150
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         150
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         190
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01645"
FT   BINDING         246
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01645"
FT   BINDING         319
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         150
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01645"
SQ   SEQUENCE   454 AA;  49488 MW;  DE1502556AD04420 CRC64;
     MNFDSIIKNG LVILENGEQE VEVGIKDGKI AAIGQDLGTS AKIIDAKGSI VSPGMIDAHV
     HITEPGGGYR DEWEGYDTGT RAAAKGGVTT FIEMPLNQVP ATVDEESIQE KFKAGKGKLS
     VDVASYGGLV PFDLDGGIQE LDSNGVVAYK CFLATCGDRS IEGDFMNVDD YSLYEGMKQI
     AKTGKILSIH AENAAITDKL GEIASKNGET SLRAYVDSRP VFTEVEPIRK IILFAKETGC
     RVHIVHIACE EGVDEIVKAQ QEGVDITCET CTHYLYFYKE ELDHIGPVVK CSPPIREQSR
     LEGMWNRVLN GDISFVTSDH SPCTPDLKAT DNAFEAWGGI AGLQNNVDVL FDEGVQKRNM
     PLSKFAAIIA TNPAKRFNLA SKGSIAVGKD ADFVFIKKDA PYELKAEDLA YRHKISPYIG
     RKIGAQVVKT ILRGVEIYDK EKGISNEKVG RFIP
//