NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Vieille C., Richardson P.;
"Complete sequence of Actinobacillus succinogenes 130Z.";
Submitted (JUN-2007) 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

CP000746; ABR74745.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001344680.1; -.

3D structure databases

ModBase

A6VP48.

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

A6VP48.

Genome annotation databases

GeneID

5348572; -.

GenomeReviews

CP000746_GR; Asuc_1385.

KEGG

asu:Asuc_1385; -.

CMR

A6VP48; Asuc_1385.

Other

ProtoNet

A6VP48.

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`	`1 340`	`340`	`Dihydroorotate dehydrogenase.`	`PRO_1000071764`
`ACT_SITE`	`178 178`		`Nucleophile (By similarity).`

Sequence information

Length: 340 AA [This is the length of the unprocessed precursor]

Molecular weight: 37055 Da [This is the MW of the unprocessed precursor]

CRC64: 887C5F00632C2B96 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLYPLIRKGI FALEPETAHN LAIKALHIAG NPWLNRALKA LLGCPQGTEK TVMGIKFKNP 

        70         80         90        100        110        120 
IGLAAGADKN GEAIDGFGAM GFGFIEVGTV TPLAQDGNAK PRQFRIVEAE GIINRNGFNN 

       130        140        150        160        170        180 
YGIDHLIENV NKSHYDGTLG INIGKNKITP IEQGKDDYIF CLNKAYNYAH YITVNISSPN 

       190        200        210        220        230        240 
TPDLRTLQYG DALDDLLKSI KERQKILAEQ YNKYVPIALK IAPDLTEAEL VQIADTVRRH 

       250        260        270        280        290        300 
QMDGVIATNT TISRDTVQGM KNAAEIGGLS GKPLQHKSTE IIRRLHRELK GDIPIIGSGG 

       310        320        330        340 
IDGVQNAQEK IAAGAELLQI YSGLIYHGPA LVKTLVQTIK

A6VP48 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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