ID   PYRC_LACGA              Reviewed;         425 AA.
AC   Q043B0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   02-SEP-2008, entry version 19.
DE   RecName: Full=Dihydroorotase;
DE            Short=DHOase;
DE            EC=3.5.2.3;
GN   Name=pyrC; OrderedLocusNames=LGAS_1089;
OS   Lactobacillus gasseri (strain ATCC 33323 / DSM 20243).
OC   Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=324831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B.,
RA   Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N.,
RA   Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K.,
RA   Goodstein D.M., Hawkins T., Plengvidhya V., Welker D., Hughes J.,
RA   Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B.,
RA   Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E.,
RA   Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C.,
RA   Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J.,
RA   Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S.,
RA   Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(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; CP000413; ABJ60462.1; -; Genomic_DNA.
DR   RefSeq; YP_814900.1; -.
DR   GeneID; 4439692; -.
DR   GenomeReviews; CP000413_GR; LGAS_1089.
DR   KEGG; lga:LGAS_1089; -.
DR   NMPDR; fig|1596.1.peg.166; -.
DR   HOGENOM; Q043B0; -.
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; 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    425       Dihydroorotase.
FT                                /FTId=PRO_1000024089.
FT   METAL        56     56       Zinc 1 (By similarity).
FT   METAL        58     58       Zinc 1 (By similarity).
FT   METAL       138    138       Zinc 1; via carbamate group (By
FT                                similarity).
FT   METAL       138    138       Zinc 2; via carbamate group (By
FT                                similarity).
FT   METAL       175    175       Zinc 2 (By similarity).
FT   METAL       228    228       Zinc 2 (By similarity).
FT   METAL       301    301       Zinc 1 (By similarity).
FT   MOD_RES     138    138       N6-carboxylysine (By similarity).
SQ   SEQUENCE   425 AA;  46019 MW;  6C2EBCDBB17D9C33 CRC64;
     MATVIKNGTV YQNGRLIKAD VLIEGKKIKA IGTDLDAEKI IDAQGMLVSP GLVDVHVHYR
     DPGQTYKEDI KTGSEAAARG GFTTVGAMPN VTPVPNTPEL MKKMVEENKH KGVVHIFQYG
     PITNDETTDI IPDYAALKKA GAFALSNDGH GVQTAQTMYL AMQKAKENNL IIATHAQDDS
     LFNKGIVNEG VAAKKLDLPP VTELAETTQI ARDLLLAQKT GVHYHICHVS TKTSVELVRL
     AKARGINVTC EVAPHHILLT DSDIPKDNGY FKMNPPLRNK EDQAALLVGL LDGTIDLIAT
     DHAPHAKSEK QGGMKNAAFG ITGSETAFST LYTKFVKEEK VLSLEQLLAL LSDKPAKVFG
     IENAGVLEPG KNADVAIFDI EHKNEIKEAD FKSKGVNTPF TGQKVYGETV MTLVDGEVVY
     QRGTK
//