Reviewed, UniProtKB/Swiss-Prot Q47741 (PYRDB_ENTFA)

Names and origin

Protein names

Recommended name:
    Dihydroorotate dehydrogenase B, catalytic subunit
    EC=1.3.3.1
Alternative name(s):
    Dihydroorotate oxidase B
    DHOdehase B
      Short name=DHODase B
      Short name=DHOD B

Gene names

Name:	pyrDB
Synonyms:	pyrD, pyrD-2
Ordered Locus Names:	EF_1714

Organism

Enterococcus faecalis (Streptococcus faecalis) [Complete proteome] [HAMAP]

Taxonomic identifier

1351 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Enterococcaceae › Enterococcus

Protein attributes

Sequence length	312 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	(S)-dihydroorotate + O(2) = orotate + H(2)O(2). HAMAP MF_00224
Cofactor	Binds 1 FMN per subunit. HAMAP MF_00224
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 4/6. HAMAP MF_00224
Subunit structure	Heterotetramer of 2 pyrK and 2 pyrD subunits By similarity.
Subcellular location	CytoplasmBy similarity.
Sequence similarities	Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Cellular component	Cytoplasm
Ligand	FMN Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	'de novo' pyrimidine base biosynthetic process Inferred from electronic annotation. Source: InterPro UMP biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: HAMAP
Molecular function	dihydroorotate oxidase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 312	312	Dihydroorotate dehydrogenase B, catalytic subunit HAMAP MF_00224		PRO_0000148391
Sites
	Active site	133	1	Nucleophile By similarity
Experimental info
	Sequence conflict	81	1	E → D in AAA67066. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q47741-1 [UniParc]. Last modified April 23, 2003. Version 2. Checksum: B97956521B85541F	FASTA	312	33,093
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Generation of auxotrophic mutants of Enterococcus faecalis." Li X., Weinstock G.M., Murray B.E. J. Bacteriol. 177:6866-6873(1995) [PubMed: 7592480] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 47077 / OG1RF.
[2]	"Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis." 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. Science 299:2071-2074(2003) [PubMed: 12663927] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: V583 / ATCC 700802.
[3]	"Dihydroorotate dehydrogenase B of Enterococcus faecalis. Characterization and insights into chemical mechanism." Marcinkeviciene J., Tinney L.M., Wang K.H., Rogers M.J., Copeland R.A. Biochemistry 38:13129-13137(1999) [PubMed: 10529184] [Abstract] Cited for: CHARACTERIZATION. Strain: ATCC 29212 / DSM 2570.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U24692 Genomic DNA. Translation: AAA67066.1. AE016830 Genomic DNA. Translation: AAO81490.1.
RefSeq	NP_815420.1.
3D structure databases
HSSP	HSSP built from PDB template 1EP2 based on UniProtKB P54322.
SMR	Q47741. Positions 4-309.
ModBase	Search...
Genome annotation databases
GeneID	1200606.
GenomeReviews	Gene locus EF_1714 in contig AE016830_GR.
KEGG	efa:EF1714.
NMPDR	fig|226185.1.peg.1605.
TIGR	EF_1714.
Phylogenomic databases
HOGENOM	Q47741.
Enzyme and pathway databases
BioCyc	EFAE226185:EF_1714-MON.
Family and domain databases
HAMAP	MF_00224. [Tree]
InterPro	IPR013785. Aldolase_TIM. IPR012135. DHO_DHase_1_2. IPR005720. DHO_DHase_1_core. IPR001295. Dihydroorotate_DHase_core. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
Pfam	PF01180. DHO_dh. 1 hit. [Graphical view]
PIRSF	PIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMs	TIGR01037. pyrD_sub1_fam. 1 hit.
PROSITE	PS00911. DHODEHASE_1. 1 hit. PS00912. DHODEHASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRDB_ENTFA

Accession

Primary (citable) accession number: Q47741

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	April 23, 2003
Last modified:	November 25, 2008
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)