ID PYRD_ARATH Reviewed; 460 AA. AC P32746; Q9FMX1; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2002, sequence version 2. DT 25-NOV-2008, entry version 79. DE RecName: Full=Dihydroorotate dehydrogenase, mitochondrial; DE Short=DHOdehase; DE EC=1.3.3.1; DE AltName: Full=Dihydroorotate oxidase; DE Flags: Precursor; GN Name=PYRD; OrderedLocusNames=At5g23300; ORFNames=MKD15.16; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=93272056; PubMed=1303803; RA Minet M., Dufour M.E., Lacroute F.; RT "Complementation of Saccharomyces cerevisiae auxotrophic mutants by RT Arabidopsis thaliana cDNAs."; RL Plant J. 2:417-422(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=22260024; PubMed=12372626; DOI=10.1016/S0014-5793(02)03425-7; RA Ullrich A., Knecht W., Piskur J., Loeffler M.; RT "Plant dihydroorotate dehydrogenase differs significantly in substrate RT specificity and inhibition from the animal enzymes."; RL FEBS Lett. 529:346-350(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=98162728; PubMed=9501997; DOI=10.1093/dnares/4.6.401; RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. RT Sequence features of the regions of 1,191,918 bp covered by seventeen RT physically assigned P1 clones."; RL DNA Res. 4:401-414(1997). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14671022; DOI=10.1105/tpc.016055; RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., RA Millar A.H.; RT "Experimental analysis of the Arabidopsis mitochondrial proteome RT highlights signaling and regulatory components, provides assessment of RT targeting prediction programs, and indicates plant-specific RT mitochondrial proteins."; RL Plant Cell 16:241-256(2004). CC -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + O(2) = orotate + CC H(2)O(2). CC -!- COFACTOR: Binds 1 FAD per subunit. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; UMP from HCO(3)(-): step 4/6. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane. CC -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. CC -!- SEQUENCE CAUTION: CC Sequence=BAB11185.1; Type=Erroneous gene model prediction; CC Sequence=CAA44695.1; Type=Frameshift; Positions=431; 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; X62909; CAA44695.1; ALT_FRAME; mRNA. DR EMBL; AF454729; AAN64025.1; -; mRNA. DR EMBL; AB007648; BAB11185.1; ALT_SEQ; Genomic_DNA. DR PIR; S23762; S23762. DR RefSeq; NP_568428.1; -. DR UniGene; At.8807; -. DR HSSP; Q02127; 1D3G. DR GeneID; 832394; -. DR GenomeReviews; BA000015_GR; AT5G23300. DR KEGG; ath:AT5G23300; -. DR TAIR; At5g23300; -. DR ArrayExpress; P32746; -. DR GermOnline; AT5G23300; Arabidopsis thaliana. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-KW. DR GO; GO:0004158; F:dihydroorotate oxidase activity; IEA:InterPro. 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:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005719; DHO_DHase_2. DR InterPro; IPR001295; Dihydroorotate_DHase_core. DR Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1. DR Pfam; PF01180; DHO_dh; 1. DR TIGRFAMs; TIGR01036; pyrD_sub2; 1. DR PROSITE; PS00911; DHODEHASE_1; 1. DR PROSITE; PS00912; DHODEHASE_2; 1. PE 1: Evidence at protein level; KW Complete proteome; FAD; Flavoprotein; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Oxidoreductase; Pyrimidine biosynthesis; KW Transit peptide. FT TRANSIT 1 62 Mitochondrion (Potential). FT CHAIN 63 460 Dihydroorotate dehydrogenase, FT mitochondrial. FT /FTId=PRO_0000029889. FT ACT_SITE 277 277 Nucleophile (By similarity). SQ SEQUENCE 460 AA; 48547 MW; E8DF1C6CCEA44FFD CRC64; MAGRAATSSA KWAREFLFRR VSSNPLGATR NCSSVPGASS APKVPHFSKR GRILTGATIG LAIAGGAYVS TADEATFCGW LFNATKVVNP FFALLDAEFA HKLAVSAAAR GWVPREKRPD PAILGLEVWG RKFSNPIGLA AGFDKNAEAT EGLLGMGFGF VEVGSVTPVP QEGNPKPRIF RLSQEGAIIN RCGFNSEGIV VVAKRLGAQH GKRMLAETSA TSSSPSDDVK PGGKSGPGIL GVNLGKNKTS EDAAADYVQG VHNLSQYADY LVINVSSPNT AGLRMLQGRK QLKDLVKKVQ AARDEMQWGD EGPPPLLVKI APDLSRGELE DIAAVALALH LDGLIISNTT VSRPDAVSNN PVATETGGLS GKPLFALSTN MLRDMYTLTR GKIPLIGCGG VSSGEDAYKK IRAGATLVQL YTGFAYGGPA LIPQIKEELV KCLERDGFKS IHEAIGADHR //