ID A0A376GVK0_ENTGA Unreviewed; 371 AA.
AC A0A376GVK0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 28-JAN-2026, entry version 29.
DE SubName: Full=Dihydroorotase {ECO:0000313|EMBL:STD81702.1};
GN ORFNames=NCTC12360_00115 {ECO:0000313|EMBL:STD81702.1};
OS Enterococcus gallinarum.
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1353 {ECO:0000313|EMBL:STD81702.1, ECO:0000313|Proteomes:UP000254807};
RN [1] {ECO:0000313|EMBL:STD81702.1, ECO:0000313|Proteomes:UP000254807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12360 {ECO:0000313|EMBL:STD81702.1,
RC ECO:0000313|Proteomes:UP000254807};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; UFYW01000001; STD81702.1; -; Genomic_DNA.
DR RefSeq; WP_060814073.1; NZ_JARPZP010000001.1.
DR AlphaFoldDB; A0A376GVK0; -.
DR OrthoDB; 9796020at2; -.
DR Proteomes; UP000254807; 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 Metal-binding {ECO:0000256|PIRSR:PIRSR039004-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000254807};
KW Zinc {ECO:0000256|PIRSR:PIRSR039004-1}.
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 151
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 151
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 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT SITE 153
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-3"
FT MOD_RES 151
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-2"
SQ SEQUENCE 371 AA; 41262 MW; 758B665DE1F16C01 CRC64;
MLDMIIRQAR TLNEEVFDIG IKQGKICQIA KTIEESAQKE WTLLPNQYLS AGWIDDHVHC
FEEMSLYYDY PDQIGVAKGV TTVIDAGTTG AENIHRFYEF AQAAKTNVFA LVNISKWGIV
EQDELADLSK IKGDLITKVL NEFPDFIVGL KARMSRTVIG ENGITPLKLA KNIQKEHPGL
PLMVHIGSAP PDLADILSCL EKGDVLTHCF NGKQNGILDR QSNTIKSFVF DAYGKGVAFD
IGHGTDSFNF LVAEKAYDAN LKAASISTDI YIRNRMKGPV YDLATTMEKL AVVGYSWQEI
IEKVTLAPAR QFQLKGKGAI EEEMDADFTI FEFKEAAKVL IDSNGNKRSI DRQIIPLKTI
IGGQVYDIES D
//
