ID PYRC_LACDA Reviewed; 425 AA.
AC Q1G867;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 01-MAY-2013, entry version 53.
DE RecName: Full=Dihydroorotase;
DE Short=DHOase;
DE EC=3.5.2.3;
GN Name=pyrC; OrderedLocusNames=Ldb2111;
OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM
OS 20081).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=390333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11842 / DSM 20081;
RX PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K.,
RA Nicolas P., Robert C., Oztas S., Mangenot S., Couloux A., Loux V.,
RA Dervyn R., Bossy R., Bolotin A., Batto J.-M., Walunas T.,
RA Gibrat J.-F., Bessieres P., Weissenbach J., Ehrlich S.D., Maguin E.;
RT "The complete genome sequence of Lactobacillus bulgaricus reveals
RT extensive and ongoing reductive evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
CC -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + H(2)O = N-carbamoyl-L-
CC aspartate.
CC -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the DHOase family. Type 2 subfamily.
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DR EMBL; CR954253; CAI98849.1; -; Genomic_DNA.
DR RefSeq; YP_619723.1; NC_008054.1.
DR ProteinModelPortal; Q1G867; -.
DR STRING; 390333.Ldb2111; -.
DR EnsemblBacteria; CAI98849; CAI98849; Ldb2111.
DR GeneID; 4084392; -.
DR KEGG; ldb:Ldb2111; -.
DR PATRIC; 22219609; VBILacDel123523_1859.
DR eggNOG; COG0044; -.
DR HOGENOM; HOG000219142; -.
DR KO; K01465; -.
DR OMA; GINTPFT; -.
DR ProtClustDB; PRK09357; -.
DR BioCyc; LDEL390333:GIXG-2080-MONOMER; -.
DR UniPathway; UPA00070; UER00117.
DR GO; GO:0004151; F:dihydroorotase activity; IEA:HAMAP.
DR GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_00220_B; PyrC_type2_B; 1; -.
DR InterPro; IPR006680; Amidohydro_1.
DR InterPro; IPR004722; DHOase.
DR InterPro; IPR002195; Dihydroorotase_CS.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Metalo_hydrolase; 1.
DR TIGRFAMs; TIGR00857; pyrC_multi; 1.
DR PROSITE; PS00482; DIHYDROOROTASE_1; FALSE_NEG.
DR PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE 3: Inferred from homology;
KW Complete proteome; Hydrolase; Metal-binding; Pyrimidine biosynthesis;
KW Zinc.
FT CHAIN 1 425 Dihydroorotase.
FT /FTId=PRO_1000024087.
FT METAL 56 56 Zinc 1 (By similarity).
FT METAL 58 58 Zinc 1 (By similarity).
FT METAL 138 138 Zinc 1; via carbamate group (By
FT similarity).
FT METAL 138 138 Zinc 2; via carbamate group (By
FT similarity).
FT METAL 175 175 Zinc 2 (By similarity).
FT METAL 228 228 Zinc 2 (By similarity).
FT METAL 301 301 Zinc 1 (By similarity).
FT MOD_RES 138 138 N6-carboxylysine (By similarity).
SQ SEQUENCE 425 AA; 46291 MW; 187D96BE7C71EB33 CRC64;
MQTVIKNGTV YQNGRLIHAD VLIEDQKIKA IGTDLTGDKV IDATGKLVSP GLVDVHVHYR
DPGQTYKEDI ETGSKAAAHG GFTTVGAMPN VTPVPDTPDL MKKMVQENKQ KGIVHIFQYG
PITKNETTDE LPDYAALKKA GAFALSNDGH GVQTAQTMYL AMQEAKKNDL IVAAHAQDDS
LFNHGIVNEG EKAKELNLPP VTELAETTQI ARDLLLAEKT GVHYHICHVS TKTSVELVRM
AKACGINVTC EAAPHHLLLT EDDIPKDNGY YKMNPPLRSK EDQAALLVGL LDGTIDLIAT
DHAPHAKQEK QGGMQNAAFG ITGSETAFST LYTKFVKEDK VFTLEQLLSW LSDQPAKVFG
LKKAGVLEPG CPADVAIFDL EHETELKEKN YQSKGINTPF TGQKIYGATV MTMVDGEVVY
QRGEK
//
