(data stored in ACNUC7421 zone)

SWISSPROT: ALLB_ECOL5

ID   ALLB_ECOL5              Reviewed;         453 AA.
AC   Q0TKD0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   11-DEC-2019, entry version 84.
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=ECP_0572;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
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}.
DR   EMBL; CP000247; ABG68601.1; -; Genomic_DNA.
DR   RefSeq; WP_000006873.1; NC_008253.1.
DR   SMR; Q0TKD0; -.
DR   EnsemblBacteria; ABG68601; ABG68601; ECP_0572.
DR   KEGG; ecp:ECP_0572; -.
DR   eggNOG; ENOG4105CD3; Bacteria.
DR   eggNOG; COG0044; LUCA.
DR   HOGENOM; HOG000219146; -.
DR   KO; K01466; -.
DR   OMA; WVTAEVT; -.
DR   BioCyc; ECOL362663:G1G5S-597-MONOMER; -.
DR   UniPathway; UPA00395; UER00653.
DR   Proteomes; UP000009182; 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;
DR   PRODOM; Q0TKD0.
DR   SWISS-2DPAGE; Q0TKD0.
KW   Hydrolase; Metal-binding; Purine metabolism; Zinc.
FT   CHAIN           1..453
FT                   /note="Allantoinase"
FT                   /id="PRO_0000317679"
FT   METAL           59
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01645"
FT   METAL           61
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01645"
FT   METAL           146
FT                   /note="Zinc 1; via carbamate group"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01645"
FT   METAL           146
FT                   /note="Zinc 2; via carbamate group"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01645"
FT   METAL           186
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01645"
FT   METAL           242
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01645"
FT   METAL           315
FT                   /note="Zinc 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;  49588 MW;  BB588074A32118B0 CRC64;
     MSFDLIIKNG TVILENEARV VDIAVKDGKI AAIGQDLGDA KDVMDASGLV VSPGMVDAHT
     HISEPGRSHW EGYETGTRAA AKGGITTMIE MPLNQLPATV DRASIELKFD AAKGKLTIDA
     AQLGGLVSYN IDRLHELDEV GVVGFKCFVA TCGDRGIDND FRDVNDWQFF KGAQKLGELG
     QPVLVHCENA LICDALGEEA KREGRVTAHD YVASRPVFTE VEAIRRVLYL AKVAGCRLHV
     CHVSSPEGVE EVTRARQEGQ DVTCESCPHY FVLDTDQFEE IGTLAKCSPP IRDLENQKGM
     WEKLFNGEID CLVSDHSPCP PEMKAGNIMK AWGGIAGLQS CMDVMFDEAV QKRGMSLPMF
     GKLMATNAAD IFGLQQKGRI APGKDADFVF IQPNSSYVLT NDDLEYRHKV SPYVGRTIGA
     RITKTILRGD VIYDIEQGFP VAPKGQFILK HQQ
//

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