ID A0A3S2UVC4_9BACI Unreviewed; 365 AA.
AC A0A3S2UVC4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 18-JUN-2025, entry version 17.
DE SubName: Full=Amidohydrolase/deacetylase family metallohydrolase {ECO:0000313|EMBL:RVT59930.1};
DE EC=3.5.2.3 {ECO:0000313|EMBL:RVT59930.1};
GN ORFNames=EM808_18600 {ECO:0000313|EMBL:RVT59930.1};
OS Niallia taxi.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae; Niallia.
OX NCBI_TaxID=2499688 {ECO:0000313|EMBL:RVT59930.1, ECO:0000313|Proteomes:UP000288024};
RN [1] {ECO:0000313|EMBL:RVT59930.1, ECO:0000313|Proteomes:UP000288024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M5HDSG1-1 {ECO:0000313|EMBL:RVT59930.1,
RC ECO:0000313|Proteomes:UP000288024};
RA Tuo L.;
RT "Bacillus sp. M5HDSG1-1, whole genome shotgun sequence.";
RL Submitted (JAN-2019) 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:RVT59930.1}.
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DR EMBL; RZTZ01000008; RVT59930.1; -; Genomic_DNA.
DR RefSeq; WP_127739710.1; NZ_RZTZ01000008.1.
DR AlphaFoldDB; A0A3S2UVC4; -.
DR Proteomes; UP000288024; 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:RVT59930.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR039004-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000288024};
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 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 266
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 365 AA; 40217 MW; 1B709D1BDD989A03 CRC64;
MKDFVLHHVK RITGEEIDIV INDGKIAKIM PAGTGLGEHM IDCSGVYVSS GWIDLHVHAF
PEFNPYGDEI DKIGVNQGVT TIVDAGSCGA DRISEMAASR QKAKTNVFAF LNISSIGLQR
VDELSRLEWI DKTKVLQAVN DYKELIVGLK ARISKSVVCD NGIEPLRIAR TLSNETALPL
MVHIGSGPPF IDEIIPLLEK RDIITHYLNG KQNNLFDTQG KPLQVLKNAI ERGVHLDVGH
GTASFSFKVA QSAKRYNIGL NTISTDIYRN NRINGPVYSL ANVLTKFLSL GYSLEEVIMA
VTTNAANWLK KPELACIKVG AVANLTLFTF RNEPITLTDS EGEKREAKQR IETKGVVING
EFIEC
//
