ID   PYRD_ANADE              Reviewed;         364 AA.
AC   Q2IQI6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=Adeh_1294;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-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; CP000251; ABC81068.1; -; Genomic_DNA.
DR   RefSeq; YP_464505.1; -.
DR   GeneID; 3888688; -.
DR   GenomeReviews; CP000251_GR; Adeh_1294.
DR   KEGG; ade:Adeh_1294; -.
DR   HOGENOM; Q2IQI6; -.
DR   OMA; Q2IQI6; AALNRMG.
DR   BioCyc; ADEH290397:ADEH_1294-MON; -.
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    364       Dihydroorotate dehydrogenase.
FT                                /FTId=PRO_1000024149.
FT   ACT_SITE    178    178       Nucleophile (By similarity).
SQ   SEQUENCE   364 AA;  38378 MW;  B750C3601ADADEC6 CRC64;
     MLWPALRSVL FQLDPERVHH LAHWALHRVP PALARARRPA PVPALAVRCM GLDFDGPMGL
     AAGFDKGDVA LPGLFGLGFS HVEIGTITPR PQPGNDRPRL FRLPEHRALL NRMGFNNEGM
     EACARRLAAL PAAARLGPVG INVGKNKATP NEDAASDYLA CIERLHPYAD YLVVNISSPN
     TPGLRQLQER EALDRLLRAC VRHLAERAPG KPLLVKLAPD LSPEALDEAV DVAIAAGAAG
     IVATNTTLSR AGVERHPRAA EAGGLSGAPL ERLATEVVRR CYARAAGRVP IVGVGGVMDA
     EGAYAKIRAG ATLVQAYTGL IYGGPGFVGR VNAGLARLLE RDGFSTLSDA VGADHRQGGG
     KAAG
//