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PYRC_BACC0
ID   PYRC_BACC0              Reviewed;         428 AA.
AC   B7JJX5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=BCAH820_3902;
OS   Bacillus cereus (strain AH820).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405535;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AH820;
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 AH820.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate
CC       to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00220}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate;
CC         Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3;
CC         Evidence={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 pathway;
CC       (S)-dihydroorotate from bicarbonate: step 3/3. {ECO:0000255|HAMAP-
CC       Rule:MF_00220}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       DHOase family. Class I DHOase subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00220}.
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DR   EMBL; CP001283; ACK88888.1; -; Genomic_DNA.
DR   RefSeq; WP_001108379.1; NC_011773.1.
DR   AlphaFoldDB; B7JJX5; -.
DR   SMR; B7JJX5; -.
DR   EnsemblBacteria; ACK88888; ACK88888; BCAH820_3902.
DR   GeneID; 45023717; -.
DR   KEGG; bcu:BCAH820_3902; -.
DR   HOGENOM; CLU_015572_1_0_9; -.
DR   OMA; QHAQEPR; -.
DR   UniPathway; UPA00070; UER00117.
DR   Proteomes; UP000001363; Chromosome.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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; -; 2.
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; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR   PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Pyrimidine biosynthesis; Zinc.
FT   CHAIN           1..428
FT                   /note="Dihydroorotase"
FT                   /id="PRO_1000193092"
FT   ACT_SITE        304
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         61..63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         61
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         151
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         151
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         178
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         231
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         304
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         308
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         322..323
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
SQ   SEQUENCE   428 AA;  46656 MW;  6AA9493906CCA956 CRC64;
     MNYLFKNGRY MNEEGKIVAT DLLVQDGKIA KVAENITADN AEVIDVNGKL IAPGLVDVHV
     HLREPGGEHK ETIETGTLAA AKGGFTTICA MPNTRPVPDC REHMEDLQNR IKEKAHVNVL
     PYGAITVRQA GSEMTDFETL KELGAFAFTD DGVGVQDASM MLAAMKRAAK LNMAVVAHCE
     ENTLINKGCV HEGKFSEKHG LNGIPSVCES VHIARDILLA EAADCHYHVC HVSTKGSVRV
     IRDAKRAGIK VTAEVTPHHL VLCEDDIPSA DPNFKMNPPL RGKEDHEALI EGLLDGTIDM
     IATDHAPHTA EEKAQGIERA PFGITGFETA FPLLYTNLVK KGIITLEQLI QFLTEKPADT
     FGLEAGRLKE GRTADITIID LEQEEEIDPT TFLSKGKNTP FAGWKCQGWP VMTIVGGKIA
     WQKESALV
 
 
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