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
//