[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/s00438-004-0995-7; PubMed=15014982 [NCBI, ExPASy, EBI, Israel, Japan] Gojkovic Z., Knecht W., Zameitat E., Warneboldt J., Coutelis J.B., Pynyaha Y., Neuveglise C., Moller K., Loffler M., Piskur J.; "Horizontal gene transfer promoted evolution of the ability to propagate under anaerobic conditions in yeasts."; Mol. Genet. Genomics 271:387-393(2004).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=MMRL 2010; Hall C.R., Dietrich F.S.; "Candida albicans DHOD."; Submitted (FEB-2003) 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

AY230865; AAO74621.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY240959; AAP39962.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q02127; 1D3G. [HSSP ENTRY / PDB]

ModBase

Q874I4.

Organism-specific databases

CGD

CAL0005359; URA1.

Ontologies

GO:0005743;	Cellular component: mitochondrial inner membrane (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.

Family and domain databases

InterPro

IPR013785; Aldolase_TIM.
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.

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

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 ?`		`Mitochondrion (Potential).`
`CHAIN`	`? 444`		`Dihydroorotate dehydrogenase, mitochondrial.`	`PRO_0000029891`
`ACT_SITE`	`257 257`		`Nucleophile (By similarity).`

Sequence information

Length: 444 AA [This is the length of the unprocessed precursor]

Molecular weight: 48426 Da [This is the MW of the unprocessed precursor]

CRC64: CD37C62FFA2E6902 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFRPSIKFKQ STLSIIARRL KSSAQHQPLR SSFVPSPIVF VAGLAVAAVG GYYCLDSRSA 

        70         80         90        100        110        120 
IHEYVLCPLI RTFTDAESGH KLGIFFMKYG LSPRLLDDGK NDQSDVLGVQ VFGHKLKNPI 

       130        140        150        160        170        180 
GLAAGLDKDG EAIESLFNCG FSYVEIGSIT PEPQPGNPQP RFFRLPKDDA VINRYGFNSS 

       190        200        210        220        230        240 
GHFNVLATLK LRFNKLLNKF GTSHSSEQHP FSNAFQQGKL LGINLGKNKF GDEVNDYVKG 

       250        260        270        280        290        300 
VERLGPYADV LVINVSSPNT PGLRDLQSEA KLTNLLTTVV KERNVLGKNL LGNKPPVLVK 

       310        320        330        340        350        360 
VAPDLTEPEI ESIANSAKEA KVDGIIISNT TIQRPVDRLL TTDKQLINQA GGLSGKPLKP 

       370        380        390        400        410        420 
LSLKALRTLR KYTKDSDLVL IGCGGISNGK DALEFGKAGA TFIELYTAFA YKGPGLVGKI 

       430        440 
RDELAEELRK EGKTWEQIIG SDDK

Q874I4 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