NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/ng.2007.38; PubMed=18037886 [NCBI, ExPASy, EBI, Israel, Japan]
Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.;
"Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors.";
Nat. Genet. 39:1469-1476(2007).

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

AM260525; CAK01023.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001609018.1; -.

3D structure databases

ModBase

A9IQ81.

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

A9IQ81.

Genome annotation databases

GeneID

5829298; -.

GenomeReviews

AM260525_GR; BT0576.

CMR

A9IQ81; BT0576.

Other

ProtoNet

A9IQ81.

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`	`1 360`	`360`	`Dihydroorotate dehydrogenase.`	`PRO_0000336456`
`ACT_SITE`	`171 171`		`Nucleophile (By similarity).`

Sequence information

Length: 360 AA [This is the length of the unprocessed precursor]

Molecular weight: 39905 Da [This is the MW of the unprocessed precursor]

CRC64: 8A403EC0D4EF371F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSFFRCIGRS ALFMLDPEHA HRLAIVGLKS GLNGCQKVVD KRLSVTIAGL KFKNFIGLAA 

        70         80         90        100        110        120 
GFDKNAEVVD EIFRLGFGFT EIGTVTPKPQ IGNPKPRLFR LKEDEAIINR MGFNNDGHQV 

       130        140        150        160        170        180 
VDDRLRICKK AGVVGVNIGA NKDTVDKIDD YTVGIAHFYD VADYFTVNIS SPNTPGLRDL 

       190        200        210        220        230        240 
QARDSLHLLL NAISKARKEQ EKKHGFSIPI FLKIAPDLSE KELDDIAEEI KLSDFDGLIV 

       250        260        270        280        290        300 
SNTTLSRQGL NNSHFSNEEG GLSGRPLFER STIVLAKMRQ KLGKEIAIIG VGGVKDAQTA 

       310        320        330        340        350        360 
LEKVKAGADL IQLYSGMVYE GPNLVITILK EILQMMQQDG VDNIKDYRDH NLEHWAKFPL

A9IQ81 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