ID PYRC_SHEB2 Reviewed; 343 AA.
AC B8E4P5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 01-MAY-2013, entry version 29.
DE RecName: Full=Dihydroorotase;
DE Short=DHOase;
DE EC=3.5.2.3;
GN Name=pyrC; OrderedLocusNames=Sbal223_1016;
OS Shewanella baltica (strain OS223).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=407976;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS223;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L.,
RA Brettin T., Detter J.C., Han C., Kuske C.R., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Brettar I., Rodrigues J.,
RA Konstantinidis K., Tiedje J.;
RT "Complete sequence of chromosome of Shewanella baltica OS223.";
RL Submitted (DEC-2008) 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; CP001252; ACK45531.1; -; Genomic_DNA.
DR RefSeq; YP_002356954.1; NC_011663.1.
DR ProteinModelPortal; B8E4P5; -.
DR SMR; B8E4P5; 3-343.
DR STRING; 407976.Sbal223_1016; -.
DR EnsemblBacteria; ACK45531; ACK45531; Sbal223_1016.
DR GeneID; 7087789; -.
DR KEGG; sbp:Sbal223_1016; -.
DR PATRIC; 23478082; VBISheBal125792_1056.
DR eggNOG; COG0418; -.
DR HOGENOM; HOG000256259; -.
DR KO; K01465; -.
DR OMA; MTLYLTE; -.
DR ProtClustDB; PRK05451; -.
DR BioCyc; SBAL407976:GJ6Y-1038-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 1 343 Dihydroorotase.
FT /FTId=PRO_1000193082.
FT METAL 13 13 Zinc 1 (By similarity).
FT METAL 15 15 Zinc 1 (By similarity).
FT METAL 99 99 Zinc 1; via carbamate group (By
FT similarity).
FT METAL 99 99 Zinc 2; via carbamate group (By
FT similarity).
FT METAL 136 136 Zinc 2 (By similarity).
FT METAL 174 174 Zinc 2 (By similarity).
FT METAL 247 247 Zinc 1 (By similarity).
FT MOD_RES 99 99 N6-carboxylysine (By similarity).
SQ SEQUENCE 343 AA; 37692 MW; 11479593A52B1EE2 CRC64;
MTTITITRPD DWHIHLRDGA QLKDTVRDIS RYMGRAIVMP NLVPPAIDTE TALTYYDRIK
AQVPAGSQFE PLMVLYLTDK TSPDEIRKAK ASGKIVAAKL YPAGATTNSD SGVTDLKNIY
PALEAMQEVG MLFLVHGEVT DSSIDIFDRE RVFIENILSK IVADFPELKI VLEHITTKDA
VDFVTQASDN VAATITAHHL LYNRNHMLAG GIRPHFYCLP ILKRNTHQQA LLAAAASGSK
KFFLGTDSAP HAKDKKEAAC GCAGSYTAHA AIELYAEAFE SVNALDKLEA FASFNGPDFY
NLPRNADTIT LVKKSWDVPA TYPLGDTNVV PIRAGEAIDW QVE
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