ID A0A250B899_9GAMM Unreviewed; 379 AA.
AC A0A250B899;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 18-JUN-2025, entry version 22.
DE SubName: Full=Dihydroorotase {ECO:0000313|EMBL:ATA22468.1};
GN ORFNames=AWC35_14680 {ECO:0000313|EMBL:ATA22468.1};
OS Gibbsiella quercinecans.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Enterobacterales; Yersiniaceae; Gibbsiella.
OX NCBI_TaxID=929813 {ECO:0000313|EMBL:ATA22468.1, ECO:0000313|Proteomes:UP000217182};
RN [1] {ECO:0000313|EMBL:ATA22468.1, ECO:0000313|Proteomes:UP000217182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FRB97 {ECO:0000313|EMBL:ATA22468.1,
RC ECO:0000313|Proteomes:UP000217182};
RA Oliw E.H.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP014136; ATA22468.1; -; Genomic_DNA.
DR RefSeq; WP_095849041.1; NZ_CP014136.1.
DR AlphaFoldDB; A0A250B899; -.
DR KEGG; gqu:AWC35_14680; -.
DR OrthoDB; 9796020at2; -.
DR Proteomes; UP000217182; Chromosome.
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:UP000217182};
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 269
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 379 AA; 40762 MW; 85EED3045DA072E8 CRC64;
MYDLIIRRAR LVDDSLADIA IRAGEIVAVG ALPTAAGAKR QLDLAGRYYA SAGWIDSHVH
CYPASPIYHD EPDRVGIASG VTTVIDAGST GANDIDDFYT LTRSAKTNVF AFLNISRTGI
SAQNELADMA QIDAQGVQQA VADYPDFIVG IKARMSSSVV GQNGIKPLVR AKAIQQQNHQ
LPLMVHIGNN PPDLDEIADL LTQGDIITHC YNGKPNRILT PAGELRASIQ RALKRGVLLD
VGHGSASFSF EVARQAIQLG ILPYTISSDI YCRNRINGPV YSLAAVMSKF FVCGLSLPQV
IDCVTRHAAA ALRLARKGQL RAGFDADLTL FDIRREPQVF TDSEGQTAES EQLLVPLAAV
VAGDVLLTDE GKAAHVFDL
//
