ID A0A1L8STP9_9ENTE Unreviewed; 368 AA.
AC A0A1L8STP9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 18-JUN-2025, entry version 31.
DE SubName: Full=Dihydroorotase {ECO:0000313|EMBL:OJG35477.1};
GN ORFNames=RV00_GL002662 {ECO:0000313|EMBL:OJG35477.1};
OS Enterococcus devriesei.
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=319970 {ECO:0000313|EMBL:OJG35477.1, ECO:0000313|Proteomes:UP000183700};
RN [1] {ECO:0000313|EMBL:OJG35477.1, ECO:0000313|Proteomes:UP000183700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22802 {ECO:0000313|EMBL:OJG35477.1,
RC ECO:0000313|Proteomes:UP000183700};
RA Zhong Z., Sun Z., Liu W., Zhang W., Zhang H.;
RT "Draft genome sequences of 29 type strains of Enterococci.";
RL Submitted (DEC-2014) 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:OJG35477.1}.
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DR EMBL; JXKM01000006; OJG35477.1; -; Genomic_DNA.
DR RefSeq; WP_071862565.1; NZ_JAHLOV010000006.1.
DR AlphaFoldDB; A0A1L8STP9; -.
DR STRING; 319970.RV00_GL002662; -.
DR OrthoDB; 9796020at2; -.
DR Proteomes; UP000183700; 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:UP000183700};
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 368 AA; 41087 MW; A224C983F0B2779E CRC64;
MLDLIVRNAK LIDGQKFELG ISDGKIVEVA DKIMDQCQGE LILTEDQYVS PGWIDDHVHC
YEKMTLYYDY PDEVGVKRGV TTVVDAGTTG AENIGDFCRL TKKTKTNVFA LLNISKWGIV
KQDELADLTK VQREAVQKAL EEYPDFIVGL KARMSKTVVG SSGIEPLKLA KEFQSEYSEL
PLMVHVGSAP PELSEILALM DKGDVLTHCF NGKENGIFDR NTKRIKSFVW DAYSKGIIFD
IGHGTDSFNF SVAQQALNEG MKSHSISSDI YVRNRQNGPV YDLATTMEKL FVVGYSWDEI
LKQVTEVPAR SFHLKNKGKL AVGYDADITV FTFDNSNREL VDSNGNIRSA KEVIMPVKTI
IGGQIYDN
//
