ID   PYRC_ACAM1              Reviewed;         345 AA.
AC   B0CF78;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   25-NOV-2008, entry version 8.
DE   RecName: Full=Dihydroorotase;
DE            Short=DHOase;
DE            EC=3.5.2.3;
GN   Name=pyrC; OrderedLocusNames=AM1_5644;
OS   Acaryochloris marina (strain MBIC 11017).
OC   Bacteria; Cyanobacteria; Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA   Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA   Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA   Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M.,
RA   Shimada Y., Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J.,
RA   Mimuro M., Blankenship R.E., Touchman J.W.;
RT   "Niche adaptation and genome expansion in the chlorophyll d-producing
RT   cyanobacterium Acaryochloris marina.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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; UMP from HCO(3)(-): step 3/6.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the DHOase family. Type 1 subfamily.
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DR   EMBL; CP000828; ABW30594.1; -; Genomic_DNA.
DR   RefSeq; YP_001519913.1; -.
DR   GeneID; 5684434; -.
DR   GenomeReviews; CP000828_GR; AM1_5644.
DR   KEGG; amr:AM1_5644; -.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR   GO; GO:0019856; P:pyrimidine base biosynthetic process; IEA:InterPro.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00219; -; 1.
DR   InterPro; IPR004721; DHOdimr.
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    345       Dihydroorotase.
FT                                /FTId=PRO_1000078095.
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   345 AA;  38498 MW;  F512F4502DA91F41 CRC64;
     MQKLTLTRPD DWHLHLRDGD ALKAVLPHSA RQFARAIVMP NLKPPVRTVA DAADYRNRIL
     AALPVGQTFE PLMTLYLTDN TSPEEISAAK ASKFVKAVKY YPAGATTNSD FGVTDIRKCD
     RIFAAMEQED IPLLLHGEVT DTNIDVFDRE KVFIETHLIP LVSRFPKLRV VLEHITTSEA
     VTFVLNTNEN IGATITPQHL LFSRNAIFKG GIRPHYYCLP ILKREKHRQA LLQAATSGNP
     KFFLGTDSAP HARNSKEQSC GCAGCYSALH AMELYAEAFE SANALDKLEA FASFYGPDFY
     QLPRNTKTIT LAKQTWQIPD EVPFPGTGLV PLRAGEEITW KIMDG
//