ID   PYRC_EHRCJ              Reviewed;         447 AA.
AC   Q3YRI2;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Dihydroorotase;
DE            Short=DHOase;
DE            EC=3.5.2.3;
GN   Name=pyrC; OrderedLocusNames=Ecaj_0639;
OS   Ehrlichia canis (strain Jake).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=269484;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16707693; DOI=10.1128/JB.01837-05;
RA   Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P.,
RA   Chain P., Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C.,
RA   Land M., Richardson P.M., Yu X.J., Walker D.H., McBride J.W.,
RA   Kyrpides N.C.;
RT   "The genome of the obligately intracellular bacterium Ehrlichia canis
RT   reveals themes of complex membrane structure and immune evasion
RT   strategies.";
RL   J. Bacteriol. 188:4015-4023(2006).
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; CP000107; AAZ68673.1; -; Genomic_DNA.
DR   RefSeq; YP_303271.1; -.
DR   GeneID; 3618182; -.
DR   GenomeReviews; CP000107_GR; Ecaj_0639.
DR   KEGG; ecn:Ecaj_0639; -.
DR   HOGENOM; Q3YRI2; -.
DR   OMA; Q3YRI2; CDVHPVG.
DR   BioCyc; ECAN269484:ECAJ_0639-MON; -.
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   ProDom; PD000518; DHOase; 1.
DR   TIGRFAMs; TIGR00857; pyrC_multi; 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    447       Dihydroorotase.
FT                                /FTId=PRO_0000325592.
FT   METAL        81     81       Zinc 1 (By similarity).
FT   METAL        83     83       Zinc 1 (By similarity).
FT   METAL       161    161       Zinc 1; via carbamate group (By
FT                                similarity).
FT   METAL       161    161       Zinc 2; via carbamate group (By
FT                                similarity).
FT   METAL       198    198       Zinc 2 (By similarity).
FT   METAL       252    252       Zinc 2 (By similarity).
FT   METAL       325    325       Zinc 1 (By similarity).
FT   MOD_RES     161    161       N6-carboxylysine (By similarity).
SQ   SEQUENCE   447 AA;  49115 MW;  9B695F6620AEBE43 CRC64;
     MYKQSWKLLG RGQDADFTVA YINARIIDPE SKLDIIGSLL TKGDKIVDFG QDLFNNGIPS
     TIDEVVDCNN NILMPGLIDI HVHFREPGQE HKETIHTGSK SAAAGGVTTV VCQPNTIPTI
     SSIITAKYIK MRALESAYVN IEFYASITKP DNSLSDMALL KEAGAVGFTD DGMPVMNSLT
     MRQALSYSSM LDTVVAQHAE DLNLSNNGHI NEGTVSYELG LKGIPDISES IIVNRDIALM
     KNIKNVHYHI LHVSSQDSLN IIKQAKNQGL KVTCEVTPHH LTLTEQDVIT HGTLAKINPP
     LRTENDRLSM VEGLKNGIID CIATDHAPHE VNTKELPLDT AAFGIVGLET MLPISLELYH
     NGTISLIDLL ATLTYKPANI IKVPRGRIKK GFVADLIILD LNHEWTIDIL KFASKSKNSP
     FHNRKVKGKV LRTIVSGKTT YTAVRNI
//