ID PYRC_PSEPF Reviewed; 348 AA.
AC Q3K7J8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 01-MAY-2013, entry version 56.
DE RecName: Full=Dihydroorotase;
DE Short=DHOase;
DE EC=3.5.2.3;
GN Name=pyrC; OrderedLocusNames=Pfl01_4519;
OS Pseudomonas fluorescens (strain Pf0-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=205922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pf0-1;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
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; CP000094; ABA76256.1; -; Genomic_DNA.
DR RefSeq; YP_350247.1; NC_007492.2.
DR ProteinModelPortal; Q3K7J8; -.
DR SMR; Q3K7J8; 3-343.
DR STRING; 205922.Pfl01_4519; -.
DR EnsemblBacteria; ABA76256; ABA76256; Pfl01_4519.
DR GeneID; 3717888; -.
DR KEGG; pfo:Pfl01_4519; -.
DR PATRIC; 19891196; VBIPseFlu44242_4525.
DR eggNOG; COG0418; -.
DR HOGENOM; HOG000256259; -.
DR KO; K01465; -.
DR OMA; MTLYLTE; -.
DR ProtClustDB; PRK05451; -.
DR BioCyc; PFLU205922:GJBD-4585-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_1000024038.
FT METAL 14 14 Zinc 1 (By similarity).
FT METAL 16 16 Zinc 1 (By similarity).
FT METAL 100 100 Zinc 1; via carbamate group (By
FT similarity).
FT METAL 100 100 Zinc 2; via carbamate group (By
FT similarity).
FT METAL 137 137 Zinc 2 (By similarity).
FT METAL 175 175 Zinc 2 (By similarity).
FT METAL 248 248 Zinc 1 (By similarity).
FT MOD_RES 100 100 N6-carboxylysine (By similarity).
SQ SEQUENCE 348 AA; 38480 MW; AB078C90E2570A7E CRC64;
MSDRLTLLRP DDWHIHLRDG AVLTNTVADV ARTFGRAIIM PNLVPPVRNA AEADGYRQRI
LAARPAGSRF EPLMVLYLTD RTQPEEIREA KASGFVHAAK LYPAGATTNS DSGVTSIDKI
FPVLEAMAEA GMPLLIHGEV TRGDVDVFDR EKIFIDEHMR RVVERFPTLK VVFEHITTGD
AVQFVNEASA NVGATITAHH LLYNRNHMLV GGIRPHFYCL PILKRNTHQE ALLDAATSGS
AKFFLGTDSA PHAQHAKEAA CGCAGCYTAY AAIELYAEAF EQRNALDKLE AFASLNGPRF
YGLPANTDRI TLVRDEWTAP TSLPFGELTV IPLRAGEKLR WRLLEEHA
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