ID   PYRC_LACLE              Reviewed;         427 AA.
AC   P48795;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-APR-2013, entry version 75.
DE   RecName: Full=Dihydroorotase;
DE            Short=DHOase;
DE            EC=3.5.2.3;
GN   Name=pyrC;
OS   Lactobacillus leichmannii.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=28039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 20076;
RX   PubMed=8589056; DOI=10.1016/0300-9084(96)88135-1;
RA   Schenk-Groeninger R., Becker J., Brendel M.;
RT   "Cloning, sequencing, and characterizing the Lactobacillus leichmannii
RT   pyrC gene encoding dihydroorotase.";
RL   Biochimie 77:265-272(1995).
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 2 subfamily.
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DR   EMBL; X78999; CAA55633.1; -; Genomic_DNA.
DR   PIR; T46955; T46955.
DR   ProteinModelPortal; P48795; -.
DR   MEROPS; M38.972; -.
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   HAMAP; MF_00220_B; PyrC_type2_B; 1; -.
DR   InterPro; IPR006680; Amidohydro_1.
DR   InterPro; IPR004722; DHOase.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Metalo_hydrolase; 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   Hydrolase; Metal-binding; Pyrimidine biosynthesis; Zinc.
FT   CHAIN         1    427       Dihydroorotase.
FT                                /FTId=PRO_0000147236.
FT   METAL        58     58       Zinc 1 (By similarity).
FT   METAL        60     60       Zinc 1 (By similarity).
FT   METAL       140    140       Zinc 1; via carbamate group (By
FT                                similarity).
FT   METAL       140    140       Zinc 2; via carbamate group (By
FT                                similarity).
FT   METAL       177    177       Zinc 2 (By similarity).
FT   METAL       230    230       Zinc 2 (By similarity).
FT   METAL       303    303       Zinc 1 (By similarity).
FT   MOD_RES     140    140       N6-carboxylysine (By similarity).
SQ   SEQUENCE   427 AA;  46319 MW;  1AB5BC6163C57E30 CRC64;
     MAILLKNGLV YQEGEFIKED VLISGSKIQA IGLDLPEEGA EVYDLKGKLL APGLVDIHEH
     YREPGFTYKE TIKTGSEAAS RGGFTTVCTM PNVDPIPDDL ETFEKQVALN EANSCVHLKQ
     YGAITEDLTS DKVVDMAALK EAGAFAFSND GHGIQQAGTM YEAMQEAAKV GLAICEHIQD
     DSLYHHGVMN AGKKAEELGL PGILGVSESA QLARDLVLAQ ATGVHYHACH VSTKESVELI
     RIAKEYGINV TAEATPHHLL LSEEEIDGNN GYYKMNPPLR SKEDQFALIE GMLDGTIDLI
     ATDHAPHSRE EKAGDMRKAA FGIIGNETAF ACLYTKFVKS GQMDLSLLLD LMSYQPAKLF
     GLDAGVLAPG KEADLAVFDL DHAEKLSEED YLSKGVNTPF TGQEVYGMTA LTFVSGKLVY
     KSKHFAD
//