NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 10895 / NRRL Y-1056 / CBS 109.51;
DOI=10.1126/science.1095781; PubMed=15001715 [NCBI, ExPASy, EBI, Israel, Japan]
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.;
"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome.";
Science 304:304-307(2004).

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

AE016816; AAS51193.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_983369.1; -.

3D structure databases

ModBase

Q75CE1.

Organism-specific databases

AGD

ACL035C; -.

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.

BLOCKS

Q75CE1.

Genome annotation databases

4619494; -.

fig|33169.1.peg.1014; -.

Phylogenomic databases

HOGENOM

Q75CE1; -.

Other

ProtoNet

Q75CE1.

UniRef

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

Keywords

Complete proteome; 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_0000029890`
`ACT_SITE`	`253 253`		`Nucleophile (By similarity).`

Sequence information

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

Molecular weight: 48288 Da [This is the MW of the unprocessed precursor]

CRC64: 27E890B278E04733 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSYKMFGRCR TACFRSPNLF AANKGMPLQA SVAGGASRYI IGTASVLVGA MAGFYIMNSR 

        70         80         90        100        110        120 
SAIHEYVSCP LVRLVTPDAE DGHKLGIWFL KYGLAPKLMF DKDDPVLKVE VFGKTMSNPI 

       130        140        150        160        170        180 
GCAAGLDKDG EAIDGIAQSG FGYVEIGTVT PLAQPGNPKP RFFRLPMDEA VINRYGFNSS 

       190        200        210        220        230        240 
GHKKVYDNVL SRVRQFLGAY FRDDTVNSLA LYKDKLLGIN LGKNKNGDEV EDYLRGVEKF 

       250        260        270        280        290        300 
QSLADVLVIN VSSPNTPGLR DLQQEGRLTE LLSMIVAKRN SLINEGNVLG ASTHKPPVLV 

       310        320        330        340        350        360 
KIAPDLTEPE LQSIAEAAKK SSIDGIIVSN TTIQRPDSLY TVDEELKNQA GGLSGKPVKP 

       370        380        390        400        410        420 
FALKALRTIH QYTKDTNLVL VGCGGISSGQ DAIEFAKAGA HFVQLYTAYA YRGPGLIARI 

       430        440 
KDEVTEELRN EGKTWMEIIG QDAK

Q75CE1 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