ID PYRC_SHESA Reviewed; 343 AA.
AC A0L0B8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 29-MAY-2013, entry version 43.
DE RecName: Full=Dihydroorotase;
DE Short=DHOase;
DE EC=3.5.2.3;
GN Name=pyrC; OrderedLocusNames=Shewana3_3263;
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R.,
RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Newman D., Salticov C., Konstantinidis K., Klappenback J.,
RA Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-2006) 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.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK49487.1; Type=Erroneous initiation;
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DR EMBL; CP000469; ABK49487.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_870893.1; NC_008577.1.
DR ProteinModelPortal; A0L0B8; -.
DR SMR; A0L0B8; 2-343.
DR STRING; 94122.Shewana3_3263; -.
DR EnsemblBacteria; ABK49487; ABK49487; Shewana3_3263.
DR GeneID; 4477372; -.
DR KEGG; shn:Shewana3_3263; -.
DR PATRIC; 23574508; VBISheSp134792_3620.
DR eggNOG; COG0418; -.
DR HOGENOM; HOG000256259; -.
DR KO; K01465; -.
DR ProtClustDB; PRK05451; -.
DR BioCyc; SSP94122:GJ9K-3377-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_0000325576.
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; 37816 MW; 970480BEDB230585 CRC64;
MTTLTITRPD DWHIHLRDGA QLKDTVRDIS RYMGRAIVMP NLVPPAIDTE TALAYYDRIK
AQVPAGSQFE PLMVLYLTDK TSPEEIRKAK ASGKIVAAKL YPAGATTNSD SGVTDLKNIY
PALEAMQEVG MLFLVHGEVT DSSIDIFDRE RVFIENILSK IVADFPKLKI VLEHITTKDA
VDFVTQASDN VAATITAHHL LYNRNHMLAG GIRPHFYCLP ILKRNTHQQA LLGAAASGNK
KFFLGTDSAP HAKDRKEAAC GCAGSYTAHA AIELYAEAFE SVNALDKLEA FASFNGPDFY
NLPRNSDTIT LVKKSWDVPV SYPLGDNNVV PIRAGEQIDW QVE
//
