ID PYRC_SALPB Reviewed; 348 AA.
AC A9N5P9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 01-MAY-2013, entry version 37.
DE RecName: Full=Dihydroorotase;
DE Short=DHOase;
DE EC=3.5.2.3;
GN Name=pyrC; OrderedLocusNames=SPAB_02367;
OS Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1016998;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1250 / SPB7;
RG The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V.,
RA Nash W., Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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 1 subfamily.
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DR EMBL; CP000886; ABX67749.1; -; Genomic_DNA.
DR RefSeq; YP_001588582.1; NC_010102.1.
DR ProteinModelPortal; A9N5P9; -.
DR SMR; A9N5P9; 5-347.
DR STRING; 272994.SPAB_02367; -.
DR EnsemblBacteria; ABX67749; ABX67749; SPAB_02367.
DR GeneID; 5780859; -.
DR KEGG; spq:SPAB_02367; -.
DR PATRIC; 18532102; VBISalEnt120821_1922.
DR eggNOG; COG0418; -.
DR HOGENOM; HOG000256259; -.
DR KO; K01465; -.
DR OMA; FEHITTE; -.
DR ProtClustDB; PRK05451; -.
DR BioCyc; SENT28901:GH9O-2364-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 GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR HAMAP; MF_00219; PyrC_type1; 1; -.
DR InterPro; IPR006680; Amidohydro_1.
DR InterPro; IPR004721; DHOdimr.
DR InterPro; IPR002195; Dihydroorotase_CS.
DR Pfam; PF01979; Amidohydro_1; 1.
DR PIRSF; PIRSF001237; DHOdimr; 1.
DR TIGRFAMs; TIGR00856; pyrC_dimer; 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 1 348 Dihydroorotase.
FT /FTId=PRO_1000078102.
FT METAL 17 17 Zinc 1 (By similarity).
FT METAL 19 19 Zinc 1 (By similarity).
FT METAL 103 103 Zinc 1; via carbamate group (By
FT similarity).
FT METAL 103 103 Zinc 2; via carbamate group (By
FT similarity).
FT METAL 140 140 Zinc 2 (By similarity).
FT METAL 178 178 Zinc 2 (By similarity).
FT METAL 251 251 Zinc 1 (By similarity).
FT MOD_RES 103 103 N6-carboxylysine (By similarity).
SQ SEQUENCE 348 AA; 38725 MW; 3F22B0D27C263B88 CRC64;
MTAPSQVLKI RRPDDWHVHL RDGDMLKTVV PYTSEIYGRA IVMPNLASPI TTVDAAIAYR
QRILDAVPAG HDFTPLMTCY LTDSLDADEL ERGFHEGVFT AAKLYPANAT TNSSHGVTSV
DAIMPVLERM EKLGMPLLVH GEVTHADVDI FDREARFIDT VMEPLRQRLT TLKVVFEHIT
TKDAAQYVRD GNDYLAATIT PQHLMFNRND MLVGGIRPHL YCLPILKRNI HQQALRELVA
SGFTRAFLGT DSAPHSRHRK ETSCGCAGCF NAPSALCSYA AVFEEMNALA HFEAFCSLNG
PQFYGLPVNT GWVELVRDEQ QVPENIALAD DSLVPFLAGE TVRWSVKK
//
