ID   PYRD_BACAH              Reviewed;         309 AA.
AC   A0RHQ6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=Dihydroorotate dehydrogenase;
DE            EC=1.3.3.1;
DE   AltName: Full=Dihydroorotate oxidase;
DE   AltName: Full=DHOdehase;
DE            Short=DHODase;
DE            Short=DHOD;
GN   Name=pyrD; OrderedLocusNames=BALH_3514;
OS   Bacillus thuringiensis (strain Al Hakam).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=412694;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17337577; DOI=10.1128/JB.00241-07;
RA   Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N.,
RA   Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O.,
RA   Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T.,
RA   Goodwin L.A., Green L.D., Han C.S., Hill K.K., Hitchcock P.,
RA   Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S.,
RA   Malfatti S., Martinez D., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O.,
RA   Wills P.L., Gilna P., Brettin T.S.;
RT   "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL   J. Bacteriol. 189:3680-3681(2007).
CC   -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + O(2) = orotate +
CC       H(2)O(2).
CC   -!- COFACTOR: Binds 1 FMN per subunit (By similarity).
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; UMP from HCO(3)(-): step 4/6.
CC   -!- SUBUNIT: Heterotetramer of 2 pyrK and 2 pyrD subunits (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family.
CC       Type 1 subfamily.
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DR   EMBL; CP000485; ABK86749.1; -; Genomic_DNA.
DR   RefSeq; YP_896256.1; -.
DR   SMR; A0RHQ6; 2-288.
DR   GeneID; 4544122; -.
DR   GenomeReviews; CP000485_GR; BALH_3514.
DR   KEGG; btl:BALH_3514; -.
DR   NMPDR; fig|412694.5.peg.3374; -.
DR   OMA; A0RHQ6; NSIGLQN.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004158; F:dihydroorotate oxidase activity; IEA:HAMAP.
DR   GO; GO:0006207; P:'de novo' pyrimidine base biosynthetic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006222; P:UMP biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_00224; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR012135; Dihydroorotate_DH_1_2.
DR   InterPro; IPR005720; Dihydroorotate_DH_1_core.
DR   InterPro; IPR001295; Dihydroorotate_DH_CS.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   Pfam; PF01180; DHO_dh; 1.
DR   PIRSF; PIRSF000164; DHO_oxidase; 1.
DR   TIGRFAMs; TIGR01037; pyrD_sub1_fam; 1.
DR   PROSITE; PS00911; DHODEHASE_1; 1.
DR   PROSITE; PS00912; DHODEHASE_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Flavoprotein; FMN; Oxidoreductase;
KW   Pyrimidine biosynthesis.
FT   CHAIN         1    309       Dihydroorotate dehydrogenase.
FT                                /FTId=PRO_1000024122.
FT   ACT_SITE    130    130       Nucleophile (By similarity).
SQ   SEQUENCE   309 AA;  32932 MW;  73370E39028EACE7 CRC64;
     MNRLQVELPG LSLKNPIIPA SGCFGFGREY AQFYDLSVLG SIMIKATTEQ PRYGNPTPRV
     AETPGGMLNA IGLQNPGLEK VMNSELPWLE QFDLPIIANV AGSQAEDYVA VAKEISKAPN
     VHALELNISC PNVKTGGIAF GTNPEIAADL TKRVKEVSEV PVYVKLSPNV ANIVEIAKAI
     ANAGADGLTM INTLLGMRLD LKTAKPILAN RTGGLSGPAI KPVAIRMVHE VSQAVNIPII
     GMGGIETAED VIEFFYAGAS AVAVGTANFI DPFVCPTIIE ELPALLDELG FDHISECQGR
     SWKQTCHSR
//