ID A0A078LX18_9STAP Unreviewed; 407 AA.
AC A0A078LX18;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Allantoate amidohydrolase {ECO:0000313|EMBL:CDZ99713.1};
GN Name=allC {ECO:0000313|EMBL:CDZ99713.1};
GN ORFNames=BN1048_00616 {ECO:0000313|EMBL:CDZ99713.1};
OS Jeotgalicoccus saudimassiliensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Jeotgalicoccus.
OX NCBI_TaxID=1461582 {ECO:0000313|EMBL:CDZ99713.1, ECO:0000313|Proteomes:UP000044136};
RN [1] {ECO:0000313|EMBL:CDZ99713.1, ECO:0000313|Proteomes:UP000044136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13MG44_air {ECO:0000313|EMBL:CDZ99713.1,
RC ECO:0000313|Proteomes:UP000044136};
RA Urmite Genomes Urmite Genomes;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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; CCSE01000001; CDZ99713.1; -; Genomic_DNA.
DR RefSeq; WP_035808327.1; NZ_CCSE01000001.1.
DR AlphaFoldDB; A0A078LX18; -.
DR STRING; 1461582.BN1048_00616; -.
DR MEROPS; M20.976; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_024588_6_0_9; -.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000044136; Unassembled WGS sequence.
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 AMIDOHYDROLASE; 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:0000313|EMBL:CDZ99713.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000044136};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 206..309
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 212
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 272
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 285
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 407 AA; 44696 MW; 12055B4E374AC828 CRC64;
MDIRETFEKL DKQFTSYGGL EPRGITRLLY SEEWRQAVSA LQDIFKENGL EVSSDAVGNV
SGRLVGSEFP DETIMSGSHI DTVAEGGHLD GQFGILAALV ATLYLKEKYG QPKRSIEVLS
IAEEEGSRFP YTFWGVKNFF NLQNNDDVKD IADGDGIKFV DAMRESGFDF KTDDKVRDDI
KAFVEVHIEQ GQILEKEEKQ IGVVTGIVGQ KRYTINLKGE ANHAGTTPMG YRKDAVVAFT
EIVQTLVQKA REIGDPLVIT FGSVKPVPGV VNVVPGEVEF SIDTRHIDEA ELNAFAKTVE
GTINEVSDKY GITADINLWM EQSPALMDES IVKMIEESAE KVAGGSYKVM PSGAGHDAQI
FSGYMPTGMI FVPSIGGISH NIEEATDVED LVKGIEVLAE TLYKLAY
//