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Database: UniProt
Entry: E8X8B4_SALT4
LinkDB: E8X8B4_SALT4
Original site: E8X8B4_SALT4 
ID   E8X8B4_SALT4            Unreviewed;       417 AA.
AC   E8X8B4;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Allantoate amidohydrolase {ECO:0000313|EMBL:ADX16277.1};
GN   Name=allC {ECO:0000313|EMBL:ADX16277.1};
GN   OrderedLocusNames=STM474_0548 {ECO:0000313|EMBL:ADX16277.1};
OS   Salmonella typhimurium (strain 4/74).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=909946 {ECO:0000313|EMBL:ADX16277.1, ECO:0000313|Proteomes:UP000008978};
RN   [1] {ECO:0000313|EMBL:ADX16277.1, ECO:0000313|Proteomes:UP000008978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4/74 {ECO:0000313|Proteomes:UP000008978};
RX   PubMed=21478351; DOI=10.1128/JB.00394-11;
RA   Richardson E.J., Limaye B., Inamdar H., Datta A., Manjari K.S.,
RA   Pullinger G.D., Thomson N.R., Joshi R.R., Watson M., Stevens M.P.;
RT   "Genome sequences of Salmonella enterica serovar typhimurium, Choleraesuis,
RT   Dublin, and Gallinarum strains of well- defined virulence in food-producing
RT   animals.";
RL   J. Bacteriol. 193:3162-3163(2011).
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; CP002487; ADX16277.1; -; Genomic_DNA.
DR   AlphaFoldDB; E8X8B4; -.
DR   MEROPS; M20.976; -.
DR   KEGG; seb:STM474_0548; -.
DR   PATRIC; fig|909946.3.peg.566; -.
DR   HOGENOM; CLU_024588_6_0_6; -.
DR   Proteomes; UP000008978; 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   InterPro; IPR011650; Peptidase_M20_dimer.
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; PF07687; M20_dimer; 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   Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT   DOMAIN          218..316
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   BINDING         87
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         133
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         196
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         221
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         281
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         294
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         388
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ   SEQUENCE   417 AA;  46147 MW;  5D9D002156B227B3 CRC64;
     MKQEFSMIKH FRHAIEETLP WLSSIGADPT GGMTRLLYSP EWLETQQQFK KRMAESGLET
     RFDDVGNLYG RLCGTQFPEQ VILSGSHIDT VVNGGNLDGQ FGALAAWLAL DWLKATYGAP
     LRTVEVVSMA EEEGSRFPYV FWGSKNIFGL ANPEEVRHIQ DAKGTGFVDA MQACGFTLPA
     APLAARTDIR AFVELHIEQG CVLESNGQSI GVVNAIVGQR RYTVTLNGES NHAGTTPMGY
     RRDTVHAFSR ICSQSIEKAK QHGDPLVLTF GKVEPQPNTV NVVPGKTTFT IDCRHTDAAV
     LREFTEQLEN DMRAICDEMD ISIDIDLWMD EAPVPMNAEL VAALTRLCET EQLNYRIMHS
     GAGHDAQIFA PRVPTCMIFV PSINGISHNP AERTNINDLA EGVKTLALML HQLAWQK
//
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