ALLB_ECOLU
ID ALLB_ECOLU Reviewed; 453 AA.
AC B7N966;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=ECUMN_0552;
OS Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN026 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928163; CAR11767.1; -; Genomic_DNA.
DR RefSeq; WP_000006892.1; NC_011751.1.
DR RefSeq; YP_002411315.1; NC_011751.1.
DR AlphaFoldDB; B7N966; -.
DR SMR; B7N966; -.
DR STRING; 585056.ECUMN_0552; -.
DR EnsemblBacteria; CAR11767; CAR11767; ECUMN_0552.
DR KEGG; eum:ECUMN_0552; -.
DR PATRIC; fig|585056.7.peg.760; -.
DR HOGENOM; CLU_015572_4_2_6; -.
DR OMA; WVTAEVT; -.
DR UniPathway; UPA00395; UER00653.
DR Proteomes; UP000007097; 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 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; Zinc.
FT CHAIN 1..453
FT /note="Allantoinase"
FT /id="PRO_1000186923"
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; 49545 MW; 78FF287316F32A8C 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 FVLDTEQFEE IGTLAKCSPP IRDLENQKGM
WEKLFNGEID CLVSDHSPCP PEMKAGNIME AWGGIAGLQN CMDVMFDEAV QKRGMSLPMF
GKLMATNAAD IFGLQQKGRI APGKDADFVF IQPNSSYVLT NDDLEYRHKV SPYVGRTIGA
RITKTILRGD VIYDIEQGFP VAPKGQFILK HQQ
