[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 200963 / HA 63 / NRRL Y-8281; Hall C.R., Dietrich F.S.; Submitted (OCT-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

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Cross-references

Sequence databases

EMBL

AY444339; AAR17522.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q6SZS6.

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`	`? 446`		`Dihydroorotate dehydrogenase, mitochondrial.`	`PRO_0000029894`
`ACT_SITE`	`255 255`		`Nucleophile (By similarity).`

Sequence information

Length: 446 AA [This is the length of the unprocessed precursor]

Molecular weight: 48346 Da [This is the MW of the unprocessed precursor]

CRC64: EE025A136B2DA82B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKYSFVSLLQ RGSIGSKQFI FFAKNEMSPL KAGVPGAKFL KYTVGFTLGT LAGFYLTNSR 

        70         80         90        100        110        120 
SAIHEYVSCP TVRLLTPDAE AGHKLGIWLL KYGLAPRLWF DKDEELLHVN VFGKTLTNPV 

       130        140        150        160        170        180 
GCAAGLDKDG EAIDGIFAGG FGYVEIGSVT PLPQPGNPKP RFFRLPMDEA VINRYGFNSS 

       190        200        210        220        230        240 
GHDSVVKNLQ NRVSRFINSY FCNDINAVDN LSLYQNKLLG INLGKNKNGD EVQDYLKGVE 

       250        260        270        280        290        300 
KFQKYADVLV INVSSPNTPG LRGLQKESIL TNLLSQVVAK RDSLVSSGNV LGAKTHRPPV 

       310        320        330        340        350        360 
LVKVAPDLEE EEIKAIAEAA KKSKVDGIIV SNTTIQRPAS LITEDKNLVA QAGGLSGKPL 

       370        380        390        400        410        420 
KPLSLKALKT MAHYTKGSGL VLVGCGGISS GADAIEFAKA GATMVELYTC YAYRGPGLIA 

       430        440 
RVKDEITEQL KRENKTWSQI IGEDVK

Q6SZS6 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