NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=WT-2 / G30;
DOI=10.1016/0378-1119(92)90057-V; PubMed=1452035 [NCBI, ExPASy, EBI, Israel, Japan]
Noel T., Labarere J.;
"Sequence of the URA1 gene encoding dihydroorotate dehydrogenase from the basidiomycete fungus Agrocybe aegerita.";
Gene 122:233-234(1992).

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: Cytoplasm (Probable).
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

M90295; AAA32636.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JN0453; JN0453.

3D structure databases

HSSP

Q02127; 1D3G. [HSSP ENTRY / PDB]

ModBase

P28294.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0016020;	Cellular component: membrane (inferred from electronic annotation from InterPro).
GO:0004158;	Molecular function: dihydroorotate oxidase activity (inferred from electronic annotation from InterPro).
GO:0006207;	Biological process: 'de novo' pyrimidine base biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006222;	Biological process: UMP biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.

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.

Other

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

Keywords

Cytoplasm; FAD; Flavoprotein; Oxidoreductase; Pyrimidine biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 328`	`328`	`Dihydroorotate dehydrogenase.`	`PRO_0000148499`
`ACT_SITE`	`173 173`		`Nucleophile (By similarity).`

Sequence information

Length: 328 AA [This is the length of the unprocessed precursor]

Molecular weight: 35085 Da [This is the MW of the unprocessed precursor]

CRC64: 71FA3D2A4D57EF75 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSGLFETLGR RALFAFDAEQ AHGLSIAGLK TGLVTGSAPN DLALSVKVAG LQFPNPLGMA 

        70         80         90        100        110        120 
AGYDKNAEVP DALLKLGFGF TEIGTITPRP QSGNPRPRIF RLVDDKAVIN RLGFNNEGHD 

       130        140        150        160        170        180 
AAFKRLSQRA GKSGIVGVNI GANKDAEDRI ADYVAGIRRF YQLARYFTVN ISSPNTPGLR 

       190        200        210        220        230        240 
NLQARDSLRE LLSRVLEARN EEGKMCTLKR PVFLKIAPDL ANEELDDIAA EATEQKLDGI 

       250        260        270        280        290        300 
IISNTTLSRA GLKSAGGRDE TGGLSGAPLF DRSTIVLARM RERVGPDMPL IGVGGVDSAE 

       310        320 
TALTKVKAGA RSRPALYGPD LSRPEPAY

P28294 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