NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
DOI=10.1126/science.1080029; PubMed=12663928 [NCBI, ExPASy, EBI, Israel, Japan]
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.;
"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
Science 299:2074-2076(2003).

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

AE015928; AAO75999.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_809805.1; -.

3D structure databases

HSSP

P54322; 1EP2. [HSSP ENTRY / PDB]

ModBase

Q8A9C3.

Enzyme and pathway databases

BioCyc

BTHE226186:BT_0892-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).
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.

BLOCKS

Q8A9C3.

Genome annotation databases

GeneID

1074664; -.

GenomeReviews

AE015928_GR; BT_0892.

KEGG

bth:BT_0892; -.

NMPDR

fig|226186.1.peg.892; -.

Phylogenomic databases

HOGENOM

Q8A9C3; -.

Genome annotation databases

CMR

Q8A9C3; BT_0892.

Other

ProtoNet

Q8A9C3.

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`	`1 303`	`303`	`Dihydroorotate dehydrogenase.`	`PRO_1000024131`
`ACT_SITE`	`130 130`		`Nucleophile (By similarity).`

Sequence information

Length: 303 AA [This is the length of the unprocessed precursor]

Molecular weight: 32296 Da [This is the MW of the unprocessed precursor]

CRC64: B51FAAF443050485 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MADLSVNIGE LQMKNPVMTA SGTFGYGEEF SDFIDIARIG GIIVKGTTLH KREGNPYPRM 

        70         80         90        100        110        120 
AETPSGMLNA VGLQNKGVDY FVEQIYPRIK DIQTNMIVNV SGSAIEDYVK TAEIINELDK 

       130        140        150        160        170        180 
IPAIELNISC PNVKQGGMAF GVSAKGASEV VKAVRAAYKK TLIVKLSPNV TDITEIARAA 

       190        200        210        220        230        240 
EESGADSVSL INTLLGMAID AERKRPILST VTGGMSGAAV KPIALRMVWQ VAKAVNIPVI 

       250        260        270        280        290        300 
GLGGIMNWKD AVEFMLAGAS AIQIGTANFI DPAVTIKVED GINNYLERHG CKSVKEIIGA 


LEV

Q8A9C3 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