ID   PYRD_ARTS2              Reviewed;         357 AA.
AC   A0JX31;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=Arth_2221;
OS   Arthrobacter sp. (strain FB24).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=290399;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chertkov O., Thompson S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K.,
RA   Nakatsu C.H., Richardson P.;
RT   "Complete sequence of chromosome 1 of Arthrobacter sp. FB24.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family.
CC       Type 2 subfamily.
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DR   EMBL; CP000454; ABK03601.1; -; Genomic_DNA.
DR   RefSeq; YP_831701.1; -.
DR   GeneID; 4445282; -.
DR   GenomeReviews; CP000454_GR; Arth_2221.
DR   KEGG; art:Arth_2221; -.
DR   TIGR; Arth_2221; -.
DR   OMA; A0JX31; AALNRMG.
DR   GO; GO:0005886; C:plasma membrane; 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_00225; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR012135; Dihydroorotate_DH_1_2.
DR   InterPro; IPR005719; Dihydroorotate_DH_2.
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; TIGR01036; pyrD_sub2; 1.
DR   PROSITE; PS00911; DHODEHASE_1; 1.
DR   PROSITE; PS00912; DHODEHASE_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Complete proteome; Flavoprotein; FMN; Membrane;
KW   Oxidoreductase; Pyrimidine biosynthesis.
FT   CHAIN         1    357       Dihydroorotate dehydrogenase.
FT                                /FTId=PRO_0000336453.
FT   ACT_SITE    189    189       Nucleophile (By similarity).
SQ   SEQUENCE   357 AA;  38147 MW;  ABD678D314C22CB4 CRC64;
     MRVYPTFFRL AFSWMDAERA HRIGFRAIRL AHSSGAGRVL AKFTAPAPSL QTTAFGITFP
     SPFGLAAGFD KEGHGIEALT ELGFGHVEVG TITGQAQPGN EKPRLFRLVE DKAVINRMGF
     NNDGATAVAP RLKSARAALQ RRHPGVRPVI GVNIGKSKVV ELEDAASDYL VSARSLAPAA
     DYLVVNVSSP NTPGLRLLQN VETLRPLLKA VGEEADKAAG RHVPLLVKIA PDLTDEDIDD
     VAKLALDLGL DGIIATNTTI GREGLTSDPE KIRDCGPGGL SGAPLKARSL EVLRRLKEAT
     GGSLTLVSVG GVENARDVQE RLDAGATLVQ GYTAFLYEGP FWAARINRQL AKHPARR
//