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Database: UniProt
Entry: Q8XCV8_ECO57
LinkDB: Q8XCV8_ECO57
Original site: Q8XCV8_ECO57 
ID   Q8XCV8_ECO57            Unreviewed;       411 AA.
AC   Q8XCV8; A0A0H3JBX8; A0A6M0JM96; Q7AGU7;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 146.
DE   SubName: Full=Allantoate amidohydrolase {ECO:0000313|EMBL:BAB34001.1};
GN   Name=allC {ECO:0000313|EMBL:BAB34001.1};
GN   ORFNames=ECs_0578 {ECO:0000313|EMBL:BAB34001.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB34001.1, ECO:0000313|Proteomes:UP000000558};
RN   [1] {ECO:0000313|EMBL:BAB34001.1, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC
RC   {ECO:0000313|Proteomes:UP000000558};
RX   PubMed=11258796; DOI=.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001235-1};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR001235-
CC       1};
CC   -!- SIMILARITY: Belongs to the peptidase M20 family.
CC       {ECO:0000256|ARBA:ARBA00006153}.
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DR   EMBL; BA000007; BAB34001.1; -; Genomic_DNA.
DR   RefSeq; NP_308605.1; NC_002695.1.
DR   RefSeq; WP_001301887.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8XCV8; -.
DR   STRING; 155864.Z0671; -.
DR   MEROPS; M20.976; -.
DR   GeneID; 916571; -.
DR   KEGG; ecs:ECs_0578; -.
DR   PATRIC; fig|386585.9.peg.685; -.
DR   eggNOG; COG0624; Bacteria.
DR   HOGENOM; CLU_024588_6_0_6; -.
DR   OMA; IWPHGRW; -.
DR   Proteomes; UP000000558; Chromosome.
DR   GO; GO:0047652; F:allantoate deiminase activity; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0009442; P:allantoin assimilation pathway; IEA:InterPro.
DR   CDD; cd03884; M20_bAS; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR017591; Allantoate_amidohydrolase.
DR   InterPro; IPR010158; Amidase_Cbmase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   NCBIfam; TIGR03176; AllC; 1.
DR   NCBIfam; TIGR01879; hydantase; 1.
DR   PANTHER; PTHR32494:SF5; ALLANTOATE DEIMINASE; 1.
DR   PANTHER; PTHR32494; ALLANTOATE DEIMINASE-RELATED; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF001235; Amidase_carbamoylase; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000558};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT   BINDING         81
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         127
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         190
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         215
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         275
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         288
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         382
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ   SEQUENCE   411 AA;  45620 MW;  EA902D7F9FF1A059 CRC64;
     MITHFRQTIE EALPWLSSFG ADPAGGMTRL LYSPEWLETQ QQLKKRMAAS GLETRFDEVG
     NLYGRLSGTE YPQEVILSGS HIDTVVNGGN LDGQFGALAA RLAIDWLKTQ YGAPLRTVEV
     VAMAEEEGSR FPYVFWGSKN IFGLANPDDV RNICDAKGNS FVDAMKACGF TLPDAPLTPR
     QDIKAFVELH IEQGCVLESN GQSIGVVNAI VGQRRYTVTL NGESNHAGTT PMGYRRDTVY
     AFSRICHQSI EKAKKMGDPL VLTFGKVEPR PNTVNVVPGK TTFTIDCRHT DAAVLRDFTQ
     QLENDMRAIC DEMDIRIDID LWMDEEPVPM NKDLVATLTE LCESEKLNYR VMHSGAGHDA
     QIFAPRVPTC MIFIPSINGI SHNPAERTNI TDLAEGVKTL ALMLYQLAWQ K
//
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