ID   PYRC_CHLTE              Reviewed;         439 AA.
AC   Q8KDK5;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 46.
DE   RecName: Full=Dihydroorotase;
DE            Short=DHOase;
DE            EC=3.5.2.3;
GN   Name=pyrC; OrderedLocusNames=CT1042;
OS   Chlorobium tepidum.
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobaculum.
OX   NCBI_TaxID=1097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / TLS;
RX   MEDLINE=22103685; PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M.,
RA   Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F.,
RA   Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P.,
RA   Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B.,
RA   Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M.,
RA   Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a
RT   photosynthetic, anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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 2 subfamily.
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DR   EMBL; AE006470; AAM72275.1; -; Genomic_DNA.
DR   RefSeq; NP_661933.1; -.
DR   GeneID; 1006973; -.
DR   GenomeReviews; AE006470_GR; CT1042.
DR   KEGG; cte:CT1042; -.
DR   NMPDR; fig|194439.1.peg.1027; -.
DR   TIGR; CT1042; -.
DR   HOGENOM; Q8KDK5; -.
DR   OMA; Q8KDK5; SHHQPHE.
DR   BioCyc; CTEP194439:CT_1042-MON; -.
DR   BRENDA; 3.5.2.3; 189605.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00220; -; 1.
DR   InterPro; IPR006680; Amidohydro_1.
DR   InterPro; IPR004722; DHOmult.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   TIGRFAMs; TIGR00857; pyrC_multi; 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    439       Dihydroorotase.
FT                                /FTId=PRO_0000147230.
FT   METAL        65     65       Zinc 1 (By similarity).
FT   METAL        67     67       Zinc 1 (By similarity).
FT   METAL       183    183       Zinc 2 (By similarity).
FT   METAL       246    246       Zinc 2 (By similarity).
FT   METAL       321    321       Zinc 1 (By similarity).
SQ   SEQUENCE   439 AA;  47039 MW;  71FDCBCA995B7183 CRC64;
     MSTLFLNARL LNPAENLDTV GSIKIGDDGL IEAVATGGES IPAKAEDNVI DLAGKVLAPG
     LFDMHCHFRE PGQEYKETLE TGSAAAVAGG FTGVALMPNT RPVIDSPLGV AYIRHHSAGL
     PIDLEVIGAM TVESRGEALA PYGKYASYSV KAVSDDGTAI QSSQIMRLAI EYAANFDLLL
     IQHAEDKHLT AGGIMNDGAV SAMLGLKGIP EVAEPIMIAR DLQLIAWLKK HKLNGAVAEP
     RYHVAHISTA ESVALVRKAK AAGLKVTCEV TPHHFTLTEH DLSSSIEKGN FIMKPPLASV
     ENRDALIEGL RDGTIDAIAT DHAPHAKHEK ECPPDQAAFG IIGLETSLGL TITELVDKGV
     ITLSQAIELL STNPRRIMGL ETILFRAGRK ANLTIIDPDC EWIVSESDFG SKSRNTPFMG
     RKLKGRALGI YHNSKLIMR
//