ALLB_SALTY
ID ALLB_SALTY Reviewed; 453 AA.
AC Q7CR08;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=STM0523;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; AE006468; AAL19477.1; -; Genomic_DNA.
DR RefSeq; NP_459518.1; NC_003197.2.
DR RefSeq; WP_000006865.1; NC_003197.2.
DR AlphaFoldDB; Q7CR08; -.
DR SMR; Q7CR08; -.
DR STRING; 99287.STM0523; -.
DR PaxDb; Q7CR08; -.
DR EnsemblBacteria; AAL19477; AAL19477; STM0523.
DR GeneID; 1252043; -.
DR KEGG; stm:STM0523; -.
DR PATRIC; fig|99287.12.peg.556; -.
DR HOGENOM; CLU_015572_4_2_6; -.
DR OMA; RNFVCSP; -.
DR PhylomeDB; Q7CR08; -.
DR BioCyc; SENT99287:STM0523-MON; -.
DR UniPathway; UPA00395; UER00653.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004038; F:allantoinase activity; IBA:GO_Central.
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:0006145; P:purine nucleobase catabolic process; IBA:GO_Central.
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..453
FT /note="Allantoinase"
FT /id="PRO_0000317685"
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
