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Database: UniProt
Entry: A0A1M7REB9_9BURK
LinkDB: A0A1M7REB9_9BURK
Original site: A0A1M7REB9_9BURK 
ID   A0A1M7REB9_9BURK        Unreviewed;       437 AA.
AC   A0A1M7REB9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Dihydroorotase {ECO:0000313|EMBL:SHN44489.1};
GN   ORFNames=SAMN05192549_12235 {ECO:0000313|EMBL:SHN44489.1};
OS   Duganella sacchari.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Duganella.
OX   NCBI_TaxID=551987 {ECO:0000313|EMBL:SHN44489.1, ECO:0000313|Proteomes:UP000184339};
RN   [1] {ECO:0000313|EMBL:SHN44489.1, ECO:0000313|Proteomes:UP000184339}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sac-22 {ECO:0000313|EMBL:SHN44489.1,
RC   ECO:0000313|Proteomes:UP000184339};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FRCX01000022; SHN44489.1; -; Genomic_DNA.
DR   RefSeq; WP_072790656.1; NZ_FRCX01000022.1.
DR   AlphaFoldDB; A0A1M7REB9; -.
DR   STRING; 551987.SAMN05192549_12235; -.
DR   OrthoDB; 9803027at2; -.
DR   Proteomes; UP000184339; Unassembled WGS sequence.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:InterPro.
DR   CDD; cd01317; DHOase_IIa; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR004722; DHOase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR00857; pyrC_multi; 1.
DR   PANTHER; PTHR43668; ALLANTOINASE; 1.
DR   PANTHER; PTHR43668:SF2; ALLANTOINASE; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
FT   DOMAIN          233..433
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   437 AA;  46253 MW;  CA30EFACD755CFA6 CRC64;
     MNALNKNIHI KNGHVIDPAN GIDGLNDLYI ADGKVLAVGA APAGFTADET IDAIGLIVSP
     GFVDLSARLR EPGFEYKATL QSEMQAAMQG GVTSLICPPD TDPVLDEPGL VEMLKHRARQ
     LNQAHVHPLG ALTVGLKGQS LTEMVELTGS GCIGFSQAEE PVTDTNVLLR AMQYAKTFGY
     TVWLRPQDAY IGRGGVAASG PLASRLGLSG VPVMSETIAL HTIFELMRAT GARVHLCRIS
     SSAALELIRS AKQEGLPVTC DVGVHHVHLT DADIGFFDSN ARFTPPFRSQ RDRDAIRRGL
     LDGTIDALCS DHTPVDDDEK LLPFAEASPG ATGLELLLSL TLKWAEDYAV QQDTGAQRPL
     SRALARITSE AARVAGLAAG TLSVGAVADV VLFDAGAHWT VEASALASQG KHTPFLGYNL
     AGQVKTTIVA GHVAYQR
//
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