(data stored in ACNUC7421 zone)

SWISSPROT: ALLB_ECO27

ID   ALLB_ECO27              Reviewed;         453 AA.
AC   B7UKI9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 61.
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   OrderedLocusNames=E2348C_0445;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Catalyzes the conversion of allantoin (5-
CC       ureidohydantoin) to allantoic acid by hydrolytic cleavage of the
CC       five-member hydantoin ring. {ECO:0000255|HAMAP-Rule:MF_01645}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-allantoin + H2O = allantoate + H(+);
CC         Xref=Rhea:RHEA:17029, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15678, ChEBI:CHEBI:17536; EC=3.5.2.5;
CC         Evidence={ECO:0000255|HAMAP-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;
CC       allantoate from (S)-allantoin: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01645}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01645}.
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two zinc
CC       ions. {ECO:0000255|HAMAP-Rule:MF_01645}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. Allantoinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01645}.
DR   EMBL; FM180568; CAS07993.1; -; Genomic_DNA.
DR   RefSeq; WP_000006873.1; NC_011601.1.
DR   SMR; B7UKI9; -.
DR   EnsemblBacteria; CAS07993; CAS07993; E2348C_0445.
DR   KEGG; ecg:E2348C_0445; -.
DR   KO; K01466; -.
DR   OMA; HFNEPGR; -.
DR   BioCyc; ECOL574521:E2348C_RS02335-MONOMER; -.
DR   UniPathway; UPA00395; UER00653.
DR   Proteomes; UP000008205; 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; B7UKI9.
DR   SWISS-2DPAGE; B7UKI9.
KW   Complete proteome; Hydrolase; Metal-binding; Purine metabolism; Zinc.
FT   CHAIN         1    453       Allantoinase.
FT                                /FTId=PRO_1000186917.
FT   METAL        59     59       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01645}.
FT   METAL        61     61       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01645}.
FT   METAL       146    146       Zinc 1; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01645}.
FT   METAL       146    146       Zinc 2; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01645}.
FT   METAL       186    186       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01645}.
FT   METAL       242    242       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01645}.
FT   METAL       315    315       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01645}.
FT   MOD_RES     146    146       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                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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