ID A0A430AWF2_9ENTE Unreviewed; 373 AA.
AC A0A430AWF2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JAN-2026, entry version 25.
DE SubName: Full=Amidohydrolase/deacetylase family metallohydrolase {ECO:0000313|EMBL:RSU12383.1};
GN ORFNames=CBF28_11130 {ECO:0000313|EMBL:RSU12383.1};
OS Vagococcus carniphilus.
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Vagococcus.
OX NCBI_TaxID=218144 {ECO:0000313|EMBL:RSU12383.1, ECO:0000313|Proteomes:UP000288028};
RN [1] {ECO:0000313|EMBL:RSU12383.1, ECO:0000313|Proteomes:UP000288028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS1714 {ECO:0000313|EMBL:RSU12383.1,
RC ECO:0000313|Proteomes:UP000288028};
RA Gulvik C.A.;
RT "Vagococcus spp. assemblies.";
RL Submitted (MAY-2017) 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:RSU12383.1}.
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DR EMBL; NGKB01000011; RSU12383.1; -; Genomic_DNA.
DR RefSeq; WP_126795259.1; NZ_CP060720.1.
DR AlphaFoldDB; A0A430AWF2; -.
DR GeneID; 95581112; -.
DR OrthoDB; 9796020at2; -.
DR Proteomes; UP000288028; Unassembled WGS sequence.
DR GO; GO:0019213; F:deacetylase activity; IEA:InterPro.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
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:RSU12383.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR039004-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000288028};
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 267
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 373 AA; 41395 MW; D682A3145DF38450 CRC64;
MLDLKIINGM SVKGEPIEIG IKDQKIVEVA PLVDGEALNV IDALNQYVSY GWIDSHVHCY
EKMNLYYDFP DEIGVKKGVT TVIDAGSTGE DNIKDFYLLA KEAKTNVLAL MNISKYGIIE
QDELADLSKI NEVKNKERIE ELSDFIIGIK ARMSKTVVGN NNVIPLEMAK TLQSQFDRLP
LMVHIGSAPP KLEDVLSLLE SGDIVTHCYN GKLNGILNEE GNVKEFVREA YQRGIVFDVG
HGTDSFNFNV AKEAIKEGLL CHTISTDIYH RNRENGPVFD FTTTLEKMLA MGFSLEATIE
MVTKNPANTF HLSSKGELAV GMDADITIFT LNEQEKKLTD SNGNELLIQK CITPTKCVVS
GNVYEIGDSY VDL
//
