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Database: UniProt
Entry: A0A1I1U1P7_9BURK
LinkDB: A0A1I1U1P7_9BURK
Original site: A0A1I1U1P7_9BURK 
ID   A0A1I1U1P7_9BURK        Unreviewed;       431 AA.
AC   A0A1I1U1P7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Dihydroorotase {ECO:0000313|EMBL:SFD64585.1};
GN   ORFNames=SAMN05216204_13137 {ECO:0000313|EMBL:SFD64585.1};
OS   Massilia yuzhufengensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1164594 {ECO:0000313|EMBL:SFD64585.1, ECO:0000313|Proteomes:UP000198639};
RN   [1] {ECO:0000313|EMBL:SFD64585.1, ECO:0000313|Proteomes:UP000198639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12041 {ECO:0000313|EMBL:SFD64585.1,
RC   ECO:0000313|Proteomes:UP000198639};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOLD01000031; SFD64585.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1U1P7; -.
DR   STRING; 1164594.SAMN05216204_13137; -.
DR   Proteomes; UP000198639; 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          287..427
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   431 AA;  45778 MW;  AF828312B6FC3496 CRC64;
     MRFARMKLHI KNGRIIDPAN GIDAVQDLFI DDGLIAAVGS APAGFSADNT IDATGLVVAP
     GLVDLSARLR EPGYEYKATL ESEMQAAMQG GVTTLVCPPD TDPVLDEPGL VEMLKHRARN
     LDQANVHPLG ALTMGLKGQA LTEMAELTEA GCIGFSQAEE PVLDTTVLLR AMQYAKTFGY
     TVWLRPQDAH IGRGGVAHSG PLASRLGLSG VPVMSETIAL HTIFELMRAS GARVHLCRMS
     SAAGLALVAA AKKEGLPLTC DVGVHHLHMT DADIGFFDPN ARFNPPLRSG RDRDAIRAAL
     LDGTVDAVCS DHTPVDDDEK LLPFAEASPG ATGLELLLSL VLKWAEDQHE MDALPRALAK
     VTANAARIAG LPAGTLSVGA AADVVLFDLD ARWKVERKAL ASQGKHTPFL GYELAGQVRA
     TVVRGRLAFQ R
//
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