Reviewed, UniProtKB/Swiss-Prot P32746 (PYRD_ARATH)

Names and origin

Protein names

Recommended name:
    Dihydroorotate dehydrogenase, mitochondrial
      Short name=DHOdehase
    EC=1.3.3.1
Alternative name(s):
    Dihydroorotate oxidase

Gene names

Name:	PYRD
Ordered Locus Names:	At5g23300
ORF Names:	MKD15.16

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	460 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	(S)-dihydroorotate + O2 = orotate + H2O2.
Cofactor	Binds 1 FAD per subunit.
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 4/6.
Subcellular location	Mitochondrion inner membrane. Ref.4
Sequence similarities	Belongs to the dihydroorotate dehydrogenase family.
Sequence caution	The sequence BAB11185.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAA44695.1 differs from that shown. Reason: Frameshift at position 431.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	'de novo' pyrimidine base biosynthetic process Inferred from electronic annotation. Source: InterPro UMP biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plastid Inferred from direct assay. Source: TAIR
Molecular function	dihydroorotate oxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 62	62	Mitochondrion Potential
	Chain	63 – 460	398	Dihydroorotate dehydrogenase, mitochondrial		PRO_0000029889
Sites
	Active site	277	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	P32746-1 [UniParc]. Last modified December 6, 2002. Version 2. Checksum: E8DF1C6CCEA44FFD	FASTA	460	48,547
	10 20 30 40 50 60 MAGRAATSSA KWAREFLFRR VSSNPLGATR NCSSVPGASS APKVPHFSKR GRILTGATIG 70 80 90 100 110 120 LAIAGGAYVS TADEATFCGW LFNATKVVNP FFALLDAEFA HKLAVSAAAR GWVPREKRPD 130 140 150 160 170 180 PAILGLEVWG RKFSNPIGLA AGFDKNAEAT EGLLGMGFGF VEVGSVTPVP QEGNPKPRIF 190 200 210 220 230 240 RLSQEGAIIN RCGFNSEGIV VVAKRLGAQH GKRMLAETSA TSSSPSDDVK PGGKSGPGIL 250 260 270 280 290 300 GVNLGKNKTS EDAAADYVQG VHNLSQYADY LVINVSSPNT AGLRMLQGRK QLKDLVKKVQ 310 320 330 340 350 360 AARDEMQWGD EGPPPLLVKI APDLSRGELE DIAAVALALH LDGLIISNTT VSRPDAVSNN 370 380 390 400 410 420 PVATETGGLS GKPLFALSTN MLRDMYTLTR GKIPLIGCGG VSSGEDAYKK IRAGATLVQL 430 440 450 460 YTGFAYGGPA LIPQIKEELV KCLERDGFKS IHEAIGADHR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complementation of Saccharomyces cerevisiae auxotrophic mutants by Arabidopsis thaliana cDNAs." Minet M., Dufour M.E., Lacroute F. Plant J. 2:417-422(1992) [PubMed: 1303803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Plant dihydroorotate dehydrogenase differs significantly in substrate specificity and inhibition from the animal enzymes." Ullrich A., Knecht W., Piskur J., Loeffler M. FEBS Lett. 529:346-350(2002) [PubMed: 12372626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence features of the regions of 1,191,918 bp covered by seventeen physically assigned P1 clones." Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., Tabata S. DNA Res. 4:401-414(1997) [PubMed: 9501997] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins." Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H. Plant Cell 16:241-256(2004) [PubMed: 14671022] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBLGenBankDDBJ	X62909 mRNA. Translation: CAA44695.1. Frameshift. AF454729 mRNA. Translation: AAN64025.1. AB007648 Genomic DNA. Translation: BAB11185.1. Sequence problems.
IPI	IPI00527650.
PIR	S23762.
RefSeq	NP_568428.1.
UniGene	At.8807
3D structure databases
HSSP	HSSP built from PDB template 1D3G based on UniProtKB Q02127.
ModBase	Search...
Proteomic databases
PRIDE	P32746.
Genome annotation databases
GeneID	832394.
GenomeReviews	Gene locus AT5G23300 in contig BA000015_GR.
KEGG	ath:AT5G23300.
Organism-specific databases
TAIR	At5g23300.
Phylogenomic databases
OMA	P32746. NASTELI.
Enzyme and pathway databases
BRENDA	1.3.3.1. 302. 1.3.99.11. 302.
Gene expression databases
ArrayExpress	P32746.
GermOnline	AT5G23300. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR012135. Dihydroorotate_DH_1_2. IPR005719. Dihydroorotate_DH_2. IPR001295. Dihydroorotate_DH_CS. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
Pfam	PF01180. DHO_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR01036. pyrD_sub2. 1 hit.
PROSITE	PS00911. DHODEHASE_1. 1 hit. PS00912. DHODEHASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRD_ARATH

Accession

Primary (citable) accession number: P32746
Secondary accession number(s): Q9FMX1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	December 6, 2002
Last modified:	June 16, 2009
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)