ID A0A2X3HMU3_9LIST Unreviewed; 375 AA.
AC A0A2X3HMU3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 28-JAN-2026, entry version 26.
DE SubName: Full=Dihydroorotase {ECO:0000313|EMBL:SQC72105.1};
GN ORFNames=NCTC13940_02819 {ECO:0000313|EMBL:SQC72105.1};
OS Listeria fleischmannii subsp. fleischmannii.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
OC Listeria.
OX NCBI_TaxID=1671902 {ECO:0000313|EMBL:SQC72105.1, ECO:0000313|Proteomes:UP000250257};
RN [1] {ECO:0000313|EMBL:SQC72105.1, ECO:0000313|Proteomes:UP000250257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13940 {ECO:0000313|EMBL:SQC72105.1,
RC ECO:0000313|Proteomes:UP000250257};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; UAWT01000049; SQC72105.1; -; Genomic_DNA.
DR RefSeq; WP_059140109.1; NZ_UAWT01000049.1.
DR AlphaFoldDB; A0A2X3HMU3; -.
DR Proteomes; UP000250257; 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 Zinc {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 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 152
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 152
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 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT SITE 154
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-3"
FT MOD_RES 152
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-2"
SQ SEQUENCE 375 AA; 41776 MW; 390282D4BA3865FD CRC64;
MFDILIKNAK TVDGNNLCVA IKQGKIVAVA PSIQNEKAEK IVDLKSKRFI SAGWIDNHVH
CDNDMPIYYD SPDEIGIKKG VTTIIDAGST GADTIQEFYQ HTRSAKTNVY ALINISKTGI
IAQNELANMK NIQKELVKQC VEALPHFILG LKARMSKTVV GDNNYIPLEI AKELQAELHD
LPIMVHIGSN PPELNEVLER LDKRDVLTHC FNGKENGIIN QTTKTIKECA WDAYKRGVRF
DIGHGTDSFN FKTASLAKKA GMTPFSLSTD IYYKNRESGP VFDLATTMEK LRVVGYSLEE
IMLMVTEHAA DNFHLKNKGR LEVGYDADIT IFDIVKGTKE LVDSNGNKEV TRELIIPTCT
IVGGEIYENE PISKI
//
