ALLB_BACLD
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 03-AUG-2022, entry version 111.
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; Firmicutes; 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 9375
RC / 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 9375
RC / 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;
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; 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 EnsemblBacteria; AAU22686; AAU22686; BL01094.
DR GeneID; 66216742; -.
DR KEGG; bld:BLi01126; -.
DR KEGG; bli:BL01094; -.
DR eggNOG; COG0044; Bacteria.
DR HOGENOM; CLU_015572_4_2_9; -.
DR OMA; WVTAEVT; -.
DR OrthoDB; 906155at2; -.
DR BioCyc; BLIC279010:BLI_RS05580-MON; -.
DR BRENDA; 3.5.2.5; 669.
DR UniPathway; UPA00395; UER00653.
DR Proteomes; UP000000606; Chromosome.
DR Bgee; BL01094; Expressed in ovary and 11 other 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; 2.30.40.10; -; 1.
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; 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
