[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 47077 / OG1RF; PubMed=7592480 [NCBI, ExPASy, EBI, Israel, Japan] Li X., Weinstock G.M., Murray B.E.; "Generation of auxotrophic mutants of Enterococcus faecalis."; J. Bacteriol. 177:6866-6873(1995).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=V583 / ATCC 700802; DOI=10.1126/science.1080613; PubMed=12663927 [NCBI, ExPASy, EBI, Israel, Japan] Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C., Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M., Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.; "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis."; Science 299:2071-2074(2003).
[3]	CHARACTERIZATION. STRAIN=ATCC 29212 / DSM 2570; DOI=10.1021/bi990674q; PubMed=10529184 [NCBI, ExPASy, EBI, Israel, Japan] Marcinkeviciene J., Tinney L.M., Wang K.H., Rogers M.J., Copeland R.A.; "Dihydroorotate dehydrogenase B of Enterococcus faecalis. Characterization and insights into chemical mechanism."; Biochemistry 38:13129-13137(1999).

Comments

CATALYTIC ACTIVITY: (S)-dihydroorotate + O₂ = orotate + H₂O₂.
COFACTOR: Binds 1 FMN per subunit.
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

U24692; AAA67066.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE016830; AAO81490.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_815420.1; -.

3D structure databases

HSSP

P54322; 1EP2. [HSSP ENTRY / PDB]

SMR

Q47741; 4-309.

ModBase

Q47741.

Enzyme and pathway databases

BioCyc

EFAE226185:EF_1714-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:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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

GeneID

1200606; -.

GenomeReviews

AE016830_GR; EF_1714.

KEGG

efa:EF1714; -.

NMPDR

fig|226185.1.peg.1605; -.

TIGR

EF_1714; -.

Phylogenomic databases

HOGENOM

Q47741; -.

Other

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`	`1 312`	`312`	`Dihydroorotate dehydrogenase B, catalytic subunit.`	`PRO_0000148391`
`ACT_SITE`	`133 133`		`Nucleophile (By similarity).`
`CONFLICT`	`81 81`		`E -> D (in Ref. 1; AAA67066).`

Sequence information

Length: 312 AA [This is the length of the unprocessed precursor]

Molecular weight: 33093 Da [This is the MW of the unprocessed precursor]

CRC64: B97956521B85541F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MMKNPLAVSI PGLTLKNPII PASGCFGFGE EYANYYDLDQ LGSIMIKATT PQARYGNPTP 

        70         80         90        100        110        120 
RVAETPSGML NAIGLQNPGL EVVMQEKLPK LEKYPNLPII ANVAGACEED YVAVCAKIGQ 

       130        140        150        160        170        180 
APNVKAIELN ISCPNVKHGG IAFGTDPEVA FQLTQAVKKV ASVPIYVKLS PNVTDIVPIA 

       190        200        210        220        230        240 
QAIEAGGADG FSMINTLLGM RIDLKTRKPI LANQTGGLSG PAIKPVAIRL IRQVASVSQL 

       250        260        270        280        290        300 
PIIGMGGVQT VDDVLEMFMA GASAVGVGTA NFTDPYICPK LIDGLPKRME ELGIESLEQL 

       310 
IKEVREGQQN AR

Q47741 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