NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=VF5;
DOI=10.1038/32831; PubMed=9537320 [NCBI, ExPASy, EBI, Israel, Japan]
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
Nature 392:353-358(1998).

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: Heterotetramer of 2 pyrK and 2 pyrD subunits (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 1 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

AE000657; AAC06426.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B70304; B70304.

RefSeq

NP_213021.1; -.

3D structure databases

HSSP

P54322; 1EP3. [HSSP ENTRY / PDB]

ModBase

O66461.

Enzyme and pathway databases

BioCyc

AAEO224324:AQ_046-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004158;	Molecular function: dihydroorotate oxidase activity (inferred from electronic annotation from HAMAP).
GO:0006207;	Biological process: 'de novo' pyrimidine base biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006222;	Biological process: UMP biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

HAMAP

MF_00224; -; 1.
PBIL [Tree]

InterPro

IPR013785; Aldolase_TIM.
IPR012135; DHO_DHase_1_2.
IPR005720; DHO_DHase_1_core.
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

TIGR01037; pyrD_sub1_fam; 1.

PROSITE

PS00911; DHODEHASE_1; 1.
PS00912; DHODEHASE_2; 1.

Genome annotation databases

1192658; -.

AE000657_GR; aq_046.

aae:aq_046; -.

fig|224324.1.peg.36; -.

Phylogenomic databases

HOGENOM

O66461; -.

Genome annotation databases

CMR

O66461; aq_046.

Other

ProtoNet

O66461.

UniRef

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

Keywords

Complete proteome; Cytoplasm; Flavoprotein; FMN; Oxidoreductase; Pyrimidine biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 306`	`306`	`Dihydroorotate dehydrogenase.`	`PRO_0000148386`
`ACT_SITE`	`129 129`		`Nucleophile (By similarity).`

Sequence information

Length: 306 AA [This is the length of the unprocessed precursor]

Molecular weight: 33523 Da [This is the MW of the unprocessed precursor]

CRC64: 3E1E04D8DE1FCD53 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDLSVELFGI RFKNPVWVAS GTFGYGVEAA EIYDISKLGA VVTKGLSLKE RLGNETPRIV 

        70         80         90        100        110        120 
ETPCGMLNSI GLQNPGVEKF LKEIYPKIKD VDTHFIANVF GETEEEYVEV CMALEDADKI 

       130        140        150        160        170        180 
VAYELNVSCP NVKKGGILFG HDPVILGNLV DRIKAKIKKP LLVKLSPNVT DVTEFAKVCI 

       190        200        210        220        230        240 
ENGADGLVLI NTLMGMKINI WKRKPDLATK TGGLSGPAIL PIAVRMIYQV YEKFGDRIPI 

       250        260        270        280        290        300 
IGVGGITTWE DAMEHVMAGA SAVQVGTANF YEPLAPLKVI EGIENFMKSQ NIKDFKELIG 


IAHRVE

O66461 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