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Database: UniProt
Entry: A0A1H8DNH0_9BACT
LinkDB: A0A1H8DNH0_9BACT
Original site: A0A1H8DNH0_9BACT 
ID   A0A1H8DNH0_9BACT        Unreviewed;       439 AA.
AC   A0A1H8DNH0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Dihydroorotase {ECO:0000313|EMBL:SEN08067.1};
GN   ORFNames=SAMN04488505_10836 {ECO:0000313|EMBL:SEN08067.1};
OS   Chitinophaga rupis.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=573321 {ECO:0000313|EMBL:SEN08067.1, ECO:0000313|Proteomes:UP000198984};
RN   [1] {ECO:0000313|EMBL:SEN08067.1, ECO:0000313|Proteomes:UP000198984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21039 {ECO:0000313|EMBL:SEN08067.1,
RC   ECO:0000313|Proteomes:UP000198984};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOBB01000008; SEN08067.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8DNH0; -.
DR   STRING; 573321.SAMN04488505_10836; -.
DR   Proteomes; UP000198984; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000198984}.
FT   DOMAIN          76..431
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   439 AA;  48030 MW;  0AB4B646B95B761B CRC64;
     MPCTFLDKHY SYSQVLFYSM QILIKKAVVI APNDPFSGQP MDILVADGRV SKVAAEIKAD
     NVTIITGNNL HVSMGWMDVF AHFCDPGQEH KEDLQTGSLA AARGGFTTVM IVPNTQPALH
     TKPQISYVLS NTSRGPVQVL PIGAITKNLE GTSLAEMYEM QEAGAAAFSD GIKPVQSPGL
     LLKALQYVKA FDGTIIQLPD DQSISAHGLM HEGIHSTQLG MPGKPALAEE LIIQRDLELA
     RYTGSKLHIT GVSTAKGIAL IAQAKEEGIK VTCSVTPYHL SFTDADLRNY DTHLKVNPPL
     RSEEDVAALK EAVVNGVVDC FATHHQPQDW DAKQLEFEYA KNGMIGLETC FGAIRRHIPQ
     LPLPQLIQML TINPRRIFNL PIPEFNKGEL ENLTVFEPDT NWTFTSADIA SRSKNSPYIG
     AELTGKVKAV INNNQVLFS
//
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