NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tokyo 1998;
DOI=10.1038/35024074; PubMed=10993077 [NCBI, ExPASy, EBI, Israel, Japan]
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS.";
Nature 407:81-86(2000).

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.
SEQUENCE CAUTION:
- Sequence=BAB13066.1; Type=Frameshift; Positions=46;

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

BA000003; BAB13066.1; ALT_FRAME; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_240180.1; -.

3D structure databases

HSSP

P05021; 1F76. [HSSP ENTRY / PDB]

ModBase

P57443.

Enzyme and pathway databases

BioCyc

BSP107806:BU362-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

P57443.

Genome annotation databases

GeneID

1110058; -.

GenomeReviews

BA000003_GR; BU362.

KEGG

buc:BU362; -.

Phylogenomic databases

HOGENOM

P57443; -.

Other

LinkHub

P57443; -.

Genome annotation databases

CMR

P57443; BU362.

Other

ProtoNet

P57443.

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`	`1 337`	`337`	`Dihydroorotate dehydrogenase.`	`PRO_0000148426`
`ACT_SITE`	`176 176`		`Nucleophile (By similarity).`

Sequence information

Length: 337 AA [This is the length of the unprocessed precursor]

Molecular weight: 37955 Da [This is the MW of the unprocessed precursor]

CRC64: 5CC459EB4E6AB772 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFYYFIRKLL FLLEPEKAHF LTLKYLNIKN IQFFDFFFYK TIILSKKIKC MGLIFDNKLG 

        70         80         90        100        110        120 
TAAGIDKNGE YIDALSKLGF GFIEVGTVTP LPQVGNPKPR MFRIVSMEGI INRMGFNNLG 

       130        140        150        160        170        180 
IDNLIRNIKK SNFKGIIGVN IGKNKSTSLE NSVDDYLICI EKIYCYAGYI AINISSPNTT 

       190        200        210        220        230        240 
NLRNLQYGIL FKKLLYKIKK KQKELHKKYL KYVPIAIKIS PDLSIKELVD ISKQLIRYKI 

       250        260        270        280        290        300 
DAVIATNTTL DHSSLFGLKN SSEQGGLSGL PLQKKSTNTI SILSKSLQKK IPIIGVGGIN 

       310        320        330 
SINSAKEKIE SGATLIQIYS GLVYHGPKLI KKIINHI

P57443 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