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Database: UniProt
Entry: D4KAS3_9FIRM
LinkDB: D4KAS3_9FIRM
Original site: D4KAS3_9FIRM 
ID   D4KAS3_9FIRM            Unreviewed;       396 AA.
AC   D4KAS3;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   SubName: Full=Dihydroorotase {ECO:0000313|EMBL:CBL01936.1};
DE            EC=3.5.2.3 {ECO:0000313|EMBL:CBL01936.1};
GN   ORFNames=FPR_16760 {ECO:0000313|EMBL:CBL01936.1};
OS   Faecalibacterium prausnitzii SL3/3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Faecalibacterium.
OX   NCBI_TaxID=657322 {ECO:0000313|EMBL:CBL01936.1, ECO:0000313|Proteomes:UP000007059};
RN   [1] {ECO:0000313|EMBL:CBL01936.1, ECO:0000313|Proteomes:UP000007059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL3/3 {ECO:0000313|EMBL:CBL01936.1,
RC   ECO:0000313|Proteomes:UP000007059};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Faecalibacterium prausnitzii SL3/3.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL01936.1, ECO:0000313|Proteomes:UP000007059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL3/3 {ECO:0000313|EMBL:CBL01936.1,
RC   ECO:0000313|Proteomes:UP000007059};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate
CC       to dihydroorotate. {ECO:0000256|ARBA:ARBA00002368}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       DHOase family. Class I DHOase subfamily.
CC       {ECO:0000256|ARBA:ARBA00010286}.
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DR   EMBL; FP929046; CBL01936.1; -; Genomic_DNA.
DR   RefSeq; WP_005920465.1; NC_021020.1.
DR   AlphaFoldDB; D4KAS3; -.
DR   GeneID; 75066972; -.
DR   KEGG; fpa:FPR_16760; -.
DR   PATRIC; fig|657322.3.peg.1572; -.
DR   eggNOG; COG0044; Bacteria.
DR   HOGENOM; CLU_015572_1_2_9; -.
DR   Proteomes; UP000007059; Chromosome.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR004722; DHOase.
DR   InterPro; IPR002195; Dihydroorotase_CS.
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.
DR   PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CBL01936.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          47..390
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   396 AA;  43238 MW;  EC49B1938E4BC8DE CRC64;
     MLLTNAVNTE GRPLEIYVKD GKIAAVGQDL SALAAENETV VDAGGLTVLP AFVDLHCHWR
     TPGFEYKEDI ETGSRAAAAG GYTFVNLMPN TKPVCSSAAQ AMMVEQKAAE VGLCDANQTV
     SITENFDGVS IDHLKTLPAS VKFITEDGHG VQDNATMARA FAICTQKDIT VMSHAEDMEI
     SPWDYRLAED IETVRNCWLS EYYQTRLHMC HVSTRGALDA IRMAKLRGAP VTCEVTPHHL
     WFTNDTCDYR VNPPIRTADD VEALVEGIRT GIVDAIATDH APHSEEDKLK GMAGMVGSET
     AFGVCYTKLC KQEGLPLELL VHLMSTRPAE ILGLAKGQLE PGFDADFVLV DLDTPYTVEK
     EKLHSKSHNT PFDGAQLYGK VFATIKAGKI TYQAEE
//
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