ID A0A917CIB8_9BACL Unreviewed; 366 AA.
AC A0A917CIB8;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 10.
DE SubName: Full=Dihydroorotase {ECO:0000313|EMBL:GGF89462.1};
GN ORFNames=GCM10010912_38250 {ECO:0000313|EMBL:GGF89462.1};
OS Paenibacillus albidus.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Paenibacillus.
OX NCBI_TaxID=2041023 {ECO:0000313|EMBL:GGF89462.1, ECO:0000313|Proteomes:UP000637643};
RN [1] {ECO:0000313|EMBL:GGF89462.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.16134 {ECO:0000313|EMBL:GGF89462.1};
RX PubMed=25193709;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Walter F., Albersmeier A., Kalinowski J., Ruckert C.;
RT "Complete genome sequence of Corynebacterium casei LMG S-19264T (=DSM
RT 44701T), isolated from a smear-ripened cheese.";
RL Int. J. Syst. Evol. Microbiol. 189:76-77(2014).
RN [2] {ECO:0000313|EMBL:GGF89462.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.16134 {ECO:0000313|EMBL:GGF89462.1};
RA Sun Q., Zhou Y.;
RL Submitted (SEP-2020) 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:GGF89462.1}.
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DR EMBL; BMKR01000016; GGF89462.1; -; Genomic_DNA.
DR RefSeq; WP_189027687.1; NZ_BMKR01000016.1.
DR AlphaFoldDB; A0A917CIB8; -.
DR Proteomes; UP000637643; 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:UP000637643};
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 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 267
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 366 AA; 39454 MW; 4888D8B96AD7490C CRC64;
MSEVTVLRNL RLVNGQAVDI AVQGGIITEI AEAGQAAGER GFDGSGMYVS SGWIDLHVHA
VPDFDPYGDE IDEIGVNQGV TMIVDAGSCG SDRIGAFYAE SARAMTKVYA FLNISRIGLR
QTDELSRLEW VDRDKVVQAV SAYPEFIVGL KARISQSVVK ENGIVPLKLA REMSAMTKLP
LMVHIGSGPP AIGEVLELLG NRDIITHYLN GKSNNLLDEA GQPLQGLLDA IGRGVHLDVG
HGTASFSFAV AEQAKAAHIG LNTISTDIYR NNRIHGPVYS MSNVLSKFLY LGYSLEEIIR
AVTWNAAAWL NKPELAGIRV GAQANLTLFT LEEGRKILTD SEGETREASH YIEAKGVFAN
GSLITC
//
