ID A0A8J2YEN6_9BACL Unreviewed; 369 AA.
AC A0A8J2YEN6;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 13.
DE SubName: Full=Dihydroorotase {ECO:0000313|EMBL:GGE26910.1};
GN ORFNames=GCM10011391_01590 {ECO:0000313|EMBL:GGE26910.1};
OS Pullulanibacillus camelliae.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Sporolactobacillaceae;
OC Pullulanibacillus.
OX NCBI_TaxID=1707096 {ECO:0000313|EMBL:GGE26910.1, ECO:0000313|Proteomes:UP000628775};
RN [1] {ECO:0000313|EMBL:GGE26910.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.15371 {ECO:0000313|EMBL:GGE26910.1};
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:GGE26910.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 1.15371 {ECO:0000313|EMBL:GGE26910.1};
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:GGE26910.1}.
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DR EMBL; BMIR01000001; GGE26910.1; -; Genomic_DNA.
DR RefSeq; WP_188687890.1; NZ_BMIR01000001.1.
DR AlphaFoldDB; A0A8J2YEN6; -.
DR Proteomes; UP000628775; 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:UP000628775};
KW Zinc {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 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 154
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 154
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 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 210
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 156
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-3"
FT MOD_RES 154
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-2"
SQ SEQUENCE 369 AA; 40027 MW; 56DCCED740BF8A43 CRC64;
MTDTAQDFIL SGLKRLNGGT RDILIRNGRI AEIAPGGSLS GESRIDCSDY YVSSGWIDLH
VHAFPEFDPY GDDIDEIGIK SGVTTIVDAG SCGADRIADL VALGEQATTH LLAFLNISRI
GLKRIDELSH LGWIDEQKLT RAIDTFKTSI VGLKVRMSQS VVGKSGIRPL SLARALSETT
ELPLMVHIGS APPSVDEILP YLKQGDVITH YLNGKSNGLF CENGEPRQVL RAALHRGVHL
DVGHGSASFS FKVAEAAKAH HIGLHTISTD IYRHNRLNGP VYNMANVLSK FLYLGYTLAD
VIAAVTTHAA DWLRKPELGR IQVGAPANLT LFTVKDEPIT LIDSEGEERI GTKRIEAQGV
VINGTFIKC
//
