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Database: UniProt
Entry: B7IUP8
LinkDB: B7IUP8
Original site: B7IUP8 
ID   PYRC_BACC2              Reviewed;         428 AA.
AC   B7IUP8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   30-AUG-2017, entry version 59.
DE   RecName: Full=Dihydroorotase {ECO:0000255|HAMAP-Rule:MF_00220};
DE            Short=DHOase {ECO:0000255|HAMAP-Rule:MF_00220};
DE            EC=3.5.2.3 {ECO:0000255|HAMAP-Rule:MF_00220};
GN   Name=pyrC {ECO:0000255|HAMAP-Rule:MF_00220};
GN   OrderedLocusNames=BCG9842_B1255;
OS   Bacillus cereus (strain G9842).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405531;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G9842;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus G9842.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl
CC       aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00220}.
CC   -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + H(2)O = N-carbamoyl-L-
CC       aspartate. {ECO:0000255|HAMAP-Rule:MF_00220}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00220};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00220};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
CC       {ECO:0000255|HAMAP-Rule:MF_00220}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. DHOase family. Class I DHOase subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00220}.
DR   EMBL; CP001186; ACK93450.1; -; Genomic_DNA.
DR   RefSeq; WP_001108387.1; NC_011772.1.
DR   ProteinModelPortal; B7IUP8; -.
DR   SMR; B7IUP8; -.
DR   PRIDE; B7IUP8; -.
DR   EnsemblBacteria; ACK93450; ACK93450; BCG9842_B1255.
DR   KEGG; bcg:BCG9842_B1255; -.
DR   HOGENOM; HOG000219142; -.
DR   KO; K01465; -.
DR   OMA; EYVKAFD; -.
DR   UniPathway; UPA00070; UER00117.
DR   Proteomes; UP000006744; 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:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01317; DHOase_IIa; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   HAMAP; MF_00220_B; PyrC_classI_B; 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   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; SSF51338; 2.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR00857; pyrC_multi; 1.
DR   PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR   PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Metal-binding; Pyrimidine biosynthesis;
KW   Zinc.
FT   CHAIN         1    428       Dihydroorotase.
FT                                /FTId=PRO_1000193094.
FT   REGION       61     63       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   REGION      322    323       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   ACT_SITE    304    304       {ECO:0000255|HAMAP-Rule:MF_00220}.
FT   METAL        59     59       Zinc 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00220}.
FT   METAL        61     61       Zinc 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00220}.
FT   METAL       151    151       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   METAL       151    151       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   METAL       178    178       Zinc 2; via pros nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00220}.
FT   METAL       231    231       Zinc 2; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00220}.
FT   METAL       304    304       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   BINDING      93     93       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   BINDING     277    277       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   BINDING     308    308       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
SQ   SEQUENCE   428 AA;  46656 MW;  3C0BAFD189C457F5 CRC64;
     MNYLFKNGRY MNEEGKIVAT DLLVQDGKIA KVAENITADN AEVIEVNGNL IAPGLVDVHV
     HLREPGGEHK ETIETGTLAA AKGGFTTICS MPNTRPVPDC REHMEDLQKR IKEKAHVNVL
     PYGAITVRQA GSEMTDFETL KELGAFAFTD DGVGVQDASM MLAAMKRAAK LNMAVVAHCE
     ENTLINKGCV HEGKFSEKHG LNGIPSVCES VHIARDILLA EAADCHYHVC HVSTKGSVRV
     IRDAKRAGIK VTAEVTPHHL VLCEDDIPSV DPNFKMNPPL RGKEDHAALI EGLLDGTIDM
     IATDHAPHTA EEKAQGIERA PFGITGFETA FPLLYTNLVK KGIITLEQLI QFLTEKPADT
     FGLEAGRLKE GRTADITIID LEQEEEIDPT TFLSKGKNTP FAGWKCQGWP VMTIVGGKIA
     WQKESALV
//
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