ID PYRC_MARMS Reviewed; 343 AA.
AC A6VXW9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 01-MAY-2013, entry version 42.
DE RecName: Full=Dihydroorotase;
DE Short=DHOase;
DE EC=3.5.2.3;
GN Name=pyrC; OrderedLocusNames=Mmwyl1_2376;
OS Marinomonas sp. (strain MWYL1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Marinomonas.
OX NCBI_TaxID=400668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWYL1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Johnston A.W.B., Todd J.D., Rogers R., Wexler M.,
RA Bond P.L., Li Y., Richardson P.;
RT "Complete sequence of Marinomonas sp. MWYL1.";
RL Submitted (JUN-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; CP000749; ABR71298.1; -; Genomic_DNA.
DR RefSeq; YP_001341233.1; NC_009654.1.
DR ProteinModelPortal; A6VXW9; -.
DR STRING; 400668.Mmwyl1_2376; -.
DR EnsemblBacteria; ABR71298; ABR71298; Mmwyl1_2376.
DR GeneID; 5365924; -.
DR KEGG; mmw:Mmwyl1_2376; -.
DR PATRIC; 22468169; VBIMarSp124341_2453.
DR eggNOG; COG0418; -.
DR HOGENOM; HOG000256259; -.
DR KO; K01465; -.
DR OMA; MTLYLTE; -.
DR ProtClustDB; PRK05451; -.
DR BioCyc; MSP400668:GHKD-2487-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; 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 1 343 Dihydroorotase.
FT /FTId=PRO_1000078097.
FT METAL 13 13 Zinc 1 (By similarity).
FT METAL 15 15 Zinc 1 (By similarity).
FT METAL 98 98 Zinc 1; via carbamate group (By
FT similarity).
FT METAL 98 98 Zinc 2; via carbamate group (By
FT similarity).
FT METAL 135 135 Zinc 2 (By similarity).
FT METAL 173 173 Zinc 2 (By similarity).
FT METAL 246 246 Zinc 1 (By similarity).
FT MOD_RES 98 98 N6-carboxylysine (By similarity).
SQ SEQUENCE 343 AA; 38087 MW; 39E18B159E9C9884 CRC64;
MNEITIIKPD DWHLHFRDQD MLLETVAATA RCFERAVVMP NLVPPVTTAE LALSYKERIL
AARPAGSTFM PVMTIYLTDK TSVQDIQDAK KAGVLAAKMY PAGATTNSDS GVNSLESLYP
VFEALADNGM LLLIHGEVTQ KHIDIFDREK EFIDQHMVNI VDRVPNLKVV FEHITTKDAV
DFVLAARDGV AATITPQHLL LNRNDMLDGG VRPHNYCLPV LKRSTHQQAL REVVKSGSPK
FFLGTDSAPH AKHRKESDCG CAGCYSAWSA LELYTQVFDE LGALDKLEGF ASLYGADFYG
LPRNTEKVTL VRESWEVPNS ITLPNGEPIV PFFAGKQISW KLK
//
