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Database: UniProt
Entry: A0A179ET38_ENTTH
LinkDB: A0A179ET38_ENTTH
Original site: A0A179ET38_ENTTH 
ID   A0A179ET38_ENTTH        Unreviewed;       370 AA.
AC   A0A179ET38;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   28-JAN-2026, entry version 43.
DE   SubName: Full=Dihydroorotase {ECO:0000313|EMBL:OAQ56019.1};
GN   ORFNames=A6E74_04680 {ECO:0000313|EMBL:OAQ56019.1}, ETH01_18440
GN   {ECO:0000313|EMBL:GEK37557.1};
OS   Enterococcus thailandicus.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=417368 {ECO:0000313|EMBL:OAQ56019.1, ECO:0000313|Proteomes:UP000078516};
RN   [1] {ECO:0000313|EMBL:OAQ56019.1, ECO:0000313|Proteomes:UP000078516}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0711D 46 {ECO:0000313|EMBL:OAQ56019.1,
RC   ECO:0000313|Proteomes:UP000078516};
RA   Beukers A.G., Zaheer R., Goji N., Cook S.R., Amoako K., Chaves A.V.,
RA   Ward M.P., Mcallister T.A.;
RT   "Draft genome of an Enterococcus thailandicus strain isolated from bovine
RT   feces.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GEK37557.1, ECO:0000313|Proteomes:UP000321361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101867 {ECO:0000313|EMBL:GEK37557.1,
RC   ECO:0000313|Proteomes:UP000321361};
RA   Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT   "Whole genome shotgun sequence of Enterococcus thailandicus NBRC 101867.";
RL   Submitted (JUL-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:OAQ56019.1}.
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DR   EMBL; BJUG01000009; GEK37557.1; -; Genomic_DNA.
DR   EMBL; LWMN01000011; OAQ56019.1; -; Genomic_DNA.
DR   RefSeq; WP_067482678.1; NZ_BJUG01000009.1.
DR   AlphaFoldDB; A0A179ET38; -.
DR   GeneID; 77487994; -.
DR   KEGG; eth:CK496_10135; -.
DR   PATRIC; fig|417368.6.peg.2472; -.
DR   OrthoDB; 9796020at2; -.
DR   Proteomes; UP000078516; Unassembled WGS sequence.
DR   Proteomes; UP000321361; 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:UP000078516};
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   370 AA;  41193 MW;  27227955ED447EEB CRC64;
     MFDLVIKNAK ELKGPSFEIG IENGKISQIA PKITGETKET LTLSSQQYLS AGWIDDHVHC
     FEEMTLYYDY PDKIGVEKGV TTVIDAGTTG AENIETFYRY AKQAKTNVYA LLNISKWGIV
     TQDELADLSK VQETLVKQKM NELPEFIVGI KARMSKTVVG KNGITPLDLA KKIQNENQHL
     PLMVHIGSAP PELAEVLARM EKGDVLTHCF NGKSNGILDS ETNEIKLIAK EAFAKGIIFD
     IGHGTDSFNF HVAEVAKQAN IKASSISTDI YIRNRENGPV YDLATTMEKL HVVGYSWEEI
     IEKVTKAPAE NFHLANKGQL KERFDADLTI FEFLEEPKVL TDSNGFTRTT DSQIKPVKTI
     IGGEIYDCQL
//
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