[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1186/1471-2164-6-166; PubMed=16305752 [NCBI, ExPASy, EBI, Israel, Japan] Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; "Characterization of 954 bovine full-CDS cDNA sequences."; BMC Genomics 6:166-166(2005).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Hereford; TISSUE=Thalamus; NIH - Mammalian Gene Collection (MGC) project; Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.

Comments

CATALYTIC ACTIVITY: (S)-dihydroorotate + O₂ = orotate + H₂O₂.
COFACTOR: Binds 1 FAD per subunit (By similarity).
PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 4/6 .
SUBCELLULAR LOCATION: Mitochondrion inner membrane (By similarity).
SIMILARITY: Belongs to the dihydroorotate dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BT020807; AAX08824.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC120337; AAI20338.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001015650.1; -.

UniGene

Bt.7483

3D structure databases

SMR

Q5E9W3; 32-395.

ModBase

Q5E9W3.

Family and domain databases

InterPro

IPR013785; Aldolase_TIM.
IPR012135; DHO_DHase_1_2.
IPR005719; DHO_DHase_2.
IPR001295; Dihydroorotate_DHase_core.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.

Pfam

PF01180; DHO_dh; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000164; DHO_oxidase; 1.

TIGRFAMs

TIGR01036; pyrD_sub2; 1.

PROSITE

PS00911; DHODEHASE_1; 1.
PS00912; DHODEHASE_2; 1.

BLOCKS

Q5E9W3.

Genome annotation databases

Ensembl

ENSBTAG00000019887; Bos taurus. [Contig view]

GeneID

533873; -.

KEGG

bta:533873; -.

Phylogenomic databases

HOVERGEN

Q5E9W3; -.

Other

ProtoNet

Q5E9W3.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; Pyrimidine biosynthesis; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 9`	`9`	`Mitochondrion (Potential).`
`CHAIN`	`10 395`	`386`	`Dihydroorotate dehydrogenase, mitochondrial.`	`PRO_0000233397`
`ACT_SITE`	`214 214`		`Nucleophile (By similarity).`

Sequence information

Length: 395 AA [This is the length of the unprocessed precursor]

Molecular weight: 42776 Da [This is the MW of the unprocessed precursor]

CRC64: 9D093C1641A44BD0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAWRQLKKRA QDAMVILGGG GLLFASYLTA TGDEHFYAEL LMPSLQRLLD PETAHRLAVR 

        70         80         90        100        110        120 
FTSLGLLPRT TFQDSDMLEV RVLGHKFRNP VGIAAGFDKH GEAVDGLYKM GFGFVEIGSV 

       130        140        150        160        170        180 
TPEPQEGNPR PRVFRLPEDQ AIINRYGFNS HGLSVVEHRL RARQQTQARL TEDGLPLGIN 

       190        200        210        220        230        240 
LGKNKTSVDA ASDYAEGVRV LGPLADYLVV NVSSPNTAGL RSLQGKAELR RLLTKVLQER 

       250        260        270        280        290        300 
DALKVAHKPA VLVKIAPDLT AQDKEDIASV VRELGIDGLI VTNSTVSRPA SLQGALRSEP 

       310        320        330        340        350        360 
GGLSGKPLRD LSTQTIREMY ALTQGRVPIV GVGGVSSGQD ALEKIRAGAS LVQLYTALTY 

       370        380        390 
RGPPVVGGVK RELEALLKEQ GFARVTDAIG ADHRR

Q5E9W3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools