ID   PYRD_AERPE              Reviewed;         306 AA.
AC   Q9YFI6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   16-JUN-2009, entry version 68.
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=APE_0260.1;
OS   Aeropyrum pernix.
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=56636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K1;
RX   MEDLINE=99310339; PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y.,
RA   Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H.,
RA   Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H.,
RA   Takamiya M., Masuda S., Funahashi T., Tanaka T., Kudoh Y.,
RA   Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y.,
RA   Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic
RT   crenarchaeon, Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BA000002; BAA79175.2; -; Genomic_DNA.
DR   PIR; E72784; E72784.
DR   RefSeq; NP_147090.2; -.
DR   HSSP; P54322; 1EP3.
DR   GeneID; 1445772; -.
DR   GenomeReviews; BA000002_GR; APE_0260.1.
DR   KEGG; ape:APE_0260.1; -.
DR   NMPDR; fig|272557.1.peg.197; -.
DR   HOGENOM; Q9YFI6; -.
DR   BRENDA; 1.3.3.1; 256344.
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; IPR012135; Dihydroorotate_DH_1_2.
DR   InterPro; IPR005720; Dihydroorotate_DH_1_core.
DR   InterPro; IPR001295; Dihydroorotate_DH_CS.
DR   Pfam; PF01180; DHO_dh; 1.
DR   PIRSF; PIRSF000164; DHO_oxidase; 1.
DR   TIGRFAMs; TIGR01037; pyrD_sub1_fam; 1.
DR   PROSITE; PS00911; DHODEHASE_1; FALSE_NEG.
DR   PROSITE; PS00912; DHODEHASE_2; FALSE_NEG.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Flavoprotein; FMN; Oxidoreductase;
KW   Pyrimidine biosynthesis.
FT   CHAIN         1    306       Dihydroorotate dehydrogenase.
FT                                /FTId=PRO_0000148406.
FT   ACT_SITE    132    132       Nucleophile (By similarity).
SQ   SEQUENCE   306 AA;  32121 MW;  B07059307532510D CRC64;
     MYSQPELSIS IAGLRLQRPV GNASGILGWE PREARLVEEG GGGFFVAKSV TYQPRKGYPQ
     PHLYPVAGGI VNAVGLANPG FREASKMLAQ TVEEASIPVI ASIAGGAPGE WVEMASTLEE
     AGVSAVELNL SCPHFAGGGL ELGQDPAAVA SVVSAVASTL RIPVIAKLGY SDRLVDAASK
     ALEAGARGLT LINSMRAMKI DVYAKKPVLG NRVGGLSGKP IHPIAVRAVY EVYGETRADI
     FAAGGVESWE DAVEFYLAGA KAVQVGAAFI TIGPHVLRSI VEGVRRYLWV EGFRSLQDIV
     GYAHRA
//