ID A0A7X6N1M5_9LACO Unreviewed; 368 AA.
AC A0A7X6N1M5;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 18-JUN-2025, entry version 17.
DE SubName: Full=Amidohydrolase/deacetylase family metallohydrolase {ECO:0000313|EMBL:NKZ23445.1};
DE EC=3.5.2.3 {ECO:0000313|EMBL:NKZ23445.1};
GN ORFNames=HF964_01295 {ECO:0000313|EMBL:NKZ23445.1};
OS Periweissella fabalis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Periweissella.
OX NCBI_TaxID=1070421 {ECO:0000313|EMBL:NKZ23445.1, ECO:0000313|Proteomes:UP000549765};
RN [1] {ECO:0000313|EMBL:NKZ23445.1, ECO:0000313|Proteomes:UP000549765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 61472 {ECO:0000313|EMBL:NKZ23445.1,
RC ECO:0000313|Proteomes:UP000549765};
RA Nicholson A.C.;
RT "MicrobeNet Type strains.";
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NKZ23445.1}.
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DR EMBL; JAAXPN010000001; NKZ23445.1; -; Genomic_DNA.
DR RefSeq; WP_168721240.1; NZ_JAAXPN010000001.1.
DR AlphaFoldDB; A0A7X6N1M5; -.
DR Proteomes; UP000549765; Unassembled WGS sequence.
DR GO; GO:0019213; F:deacetylase activity; IEA:InterPro.
DR GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR020043; Deacetylase_Atu3266-like.
DR InterPro; IPR047601; EF_0837-like.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR03583; EF_0837; 1.
DR NCBIfam; NF006689; PRK09237.1; 1.
DR PANTHER; PTHR42717; DIHYDROOROTASE-RELATED; 1.
DR PANTHER; PTHR42717:SF1; IMIDAZOLONEPROPIONASE AND RELATED AMIDOHYDROLASES; 1.
DR Pfam; PF22647; EF_0837-like_N; 1.
DR PIRSF; PIRSF039004; ADE_EF_0837; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:NKZ23445.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR039004-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000549765};
KW Zinc {ECO:0000256|PIRSR:PIRSR039004-1}.
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT SITE 152
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-3"
FT MOD_RES 150
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-2"
SQ SEQUENCE 368 AA; 40361 MW; 075BB6D0ADCB0EF6 CRC64;
MTETVLKGGR LITGEPFEVA YENGKLTAVG TEINPVNKTV IDITGQYLSP GWIDDHVHCF
SEMHLYYDYP DEIGVQKGVT TVIDAGTTGA ENIGRFHQLA LQAKTNVLAL VNISKWGIVE
QDELADLSKI KQALVTKVLH EYPDFIVGIK ARMSKTVIGS NGITPLKLAK EIQKTNQNLP
LMVHIGSEPP KLTEILDVME PGDVMTHCFN GKPNGILDRE TDEIKAFAKV AYEHGIIFDT
GHGTDSFNFH VAEVAFAKGI KANSISTDIY IRNRKNGPVY DLATTMEKLH VVGYTWPEII
EKVTTAPANN FHLTTKGKLV VGADADITVF DFEDGAKTLT DSNGFTRTTN VQIKPHYAII
GGACYDVL
//
