ID   PYRD_AERHH              Reviewed;         336 AA.
AC   A0KKK9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, 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=AHA_2287;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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; CP000462; ABK37752.1; -; Genomic_DNA.
DR   RefSeq; YP_856810.1; -.
DR   GeneID; 4488940; -.
DR   GenomeReviews; CP000462_GR; AHA_2287.
DR   KEGG; aha:AHA_2287; -.
DR   TIGR; AHA_2287; -.
DR   OMA; A0KKK9; NAEQQGG.
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    336       Dihydroorotate dehydrogenase.
FT                                /FTId=PRO_1000024147.
FT   ACT_SITE    175    175       Nucleophile (By similarity).
SQ   SEQUENCE   336 AA;  36360 MW;  C2D036246386BE8D CRC64;
     MLYPLARHFL FKLNPEQAHD LSIKYLPRLL GTPLDCFFRH SLPKRPVTVM GLSFANPVGL
     AAGLDKDGEC IDAFGAMGFG FIEVGTVTPR PQSGNDKPRL FRVIPAEGII NRMGFNNKGV
     DHLVAQVKKA KYQGVIGINI GKNKDTPIEQ GKDDYLICMD KVYDQAGYIA VNISSPNTPG
     LRSLQYGDAL DELLAALKVR QQELAAQYKK YVPLAVKIAP DLTPDEINQV AASLIKNGID
     GVIATNTTLE RDMIYDMPHA AEAGGLSGRP LQHKSTEVIR QLAKALDGAL PIIGVGGIDS
     AMAAREKLAA GASLVQIYSG FIYKGPDLVK EIVTHI
//