ID A0A1X6WQW2_9ENTE Unreviewed; 410 AA.
AC A0A1X6WQW2;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Allantoate amidohydrolase {ECO:0000313|EMBL:SLM86632.1};
DE EC=3.5.3.9 {ECO:0000313|EMBL:SLM86632.1};
GN ORFNames=FM121_11095 {ECO:0000313|EMBL:SLM86632.1};
OS Vagococcus fluvialis bH819.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=1255619 {ECO:0000313|EMBL:SLM86632.1, ECO:0000313|Proteomes:UP000195918};
RN [1] {ECO:0000313|Proteomes:UP000195918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bH819 {ECO:0000313|Proteomes:UP000195918};
RA Dridi B.;
RL Submitted (FEB-2017) 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; FWFD01000015; SLM86632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6WQW2; -.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000195918; Unassembled WGS sequence.
DR GO; GO:0047652; F:allantoate deiminase activity; IEA:UniProtKB-EC.
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:0000313|EMBL:SLM86632.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000195918};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 211..309
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 214
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 274
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 287
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 410 AA; 45222 MW; 2802CF744CAA9A09 CRC64;
MENFNKLVEE HVEWISSIGA DPTGGTTRLL YDENWRVAQN GLKDKFETQG LVTNFDEIGN
LYGKLSGSKY PNETILTGSH VDTVVNGGKL DGQFGIIASY LAVKYLKETH GAPLRNLEIV
SMAEEEGSRF PYAFWGSKNI WGLADKNDVI DSQDANGIKF VDAMKESGFD FRSETMPVRD
DVKAFVEIHI EQGSVLEKTG KQVGVVNNIV GQKRYTITLT GESNHAGTTP MGFRKDTVYA
MSKMISQATD LAYEVGDPLV LTFGHVEVQP NTVNVVPGHV TFSMDCRHTD KNELAEFTQK
IEKLFSEIAT AHEVEIEIDN WMNEVPVPMS SAVVKTLEEA CQEAKLNYTV MHSGAGHDSQ
IFAPQVPTAM IFVPSIGGIS HNPAEDTKTE DLVEGLKALI ASLYKLAYEE
//
