NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.;
"Complete sequence of chromosome 1 of Burkholderia sp. 383.";
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.

Comments

CATALYTIC ACTIVITY: (S)-dihydroorotate + O₂ = orotate + H₂O₂.
COFACTOR: Binds 1 FMN per subunit (By similarity).
PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 4/6 .
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein (By similarity).
SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.

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

CP000151; ABB08291.1; ALT_INIT; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_368935.1; -.

3D structure databases

ModBase

Q39GX5.

Enzyme and pathway databases

BioCyc

BSP36773:BCEP18194_A4696-MON; -.

Ontologies

GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from HAMAP).
GO:0004158;	Molecular function: dihydroorotate oxidase activity (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00225; -; 1.
PBIL [Tree]

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

Q39GX5.

Genome annotation databases

GeneID

3749902; -.

GenomeReviews

CP000151_GR; Bcep18194_A4696.

KEGG

bur:Bcep18194_A4696; -.

NMPDR

fig|269483.3.peg.6238; -.

Phylogenomic databases

HOGENOM

Q39GX5; -.

Genome annotation databases

CMR

Q39GX5; Bcep18194_A4696.

Other

ProtoNet

Q39GX5.

UniRef

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

Keywords

Cell membrane; Complete proteome; Flavoprotein; FMN; Membrane; Oxidoreductase; Pyrimidine biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 345`	`345`	`Dihydroorotate dehydrogenase.`	`PRO_0000336460`
`ACT_SITE`	`178 178`		`Nucleophile (By similarity).`

Sequence information

Length: 345 AA [This is the length of the unprocessed precursor]

Molecular weight: 36750 Da [This is the MW of the unprocessed precursor]

CRC64: CEA3CDE9EAE9640A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFSSLYPLAR ASLFKMDAED AHHLTLRALG AAGRTGLACA LSARVPDAPR TVMGLTFRNP 

        70         80         90        100        110        120 
VGLAAGLDKD GAAIDGLAAL GFGFIEVGTV TPRAQPGNPR PRMFRLPQAE ALINRMGFNN 

       130        140        150        160        170        180 
HGVDQFVKNV QAARYRGILG LNIGKNADTP IERAAEDYLY CLERVYPFAS YVTINISSPN 

       190        200        210        220        230        240 
TKNLRQLQGA GELDALLAAL KDKQQRLADL HGKLVPLALK IAPDLDDEQV KEIGDTLLRH 

       250        260        270        280        290        300 
KIEAVIATNT TLSRAAVQGL PHADEAGGLS GRPVFDASNE VIRKLHAEVG SEVPIIGVGG 

       310        320        330        340 
IFSGEDARAK LAAGAALVQL YTGFIYRGPA LVSECVKAIA RERTA

Q39GX5 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