Q1G864 (PYRDA_LACDA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydroorotate dehydrogenase A (fumarate)
Short name=DHOD A
Short name=DHODase A
Short name=DHOdehase A
EC=1.3.98.1

Gene names

Name:	pyrD
Ordered Locus Names:	Ldb2114

Organism

Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081) [Complete proteome] [HAMAP]

Taxonomic identifier

390333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Lactobacillaceae › Lactobacillus › Lactobacillus delbrueckii › Lactobacillus delbrueckii subsp. bulgaricus

Protein attributes

Sequence length	307 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor By similarity. HAMAP-Rule MF_00224
Catalytic activity	(S)-dihydroorotate + fumarate = orotate + succinate. HAMAP-Rule MF_00224
Cofactor	Binds 1 FMN per subunit By similarity.
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway. HAMAP-Rule MF_00224
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By 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' UMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway 'de novo' pyrimidine nucleobase biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	dihydroorotate oxidase (fumarate) activity Inferred from electronic annotation. Source: EC dihydroorotate oxidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 307	307	Dihydroorotate dehydrogenase A (fumarate) HAMAP-Rule MF_00224		PRO_1000024135
Regions
	Nucleotide binding	46 – 47	2	FMN By similarity
	Nucleotide binding	246 – 247	2	FMN By similarity
	Nucleotide binding	268 – 269	2	FMN By similarity
	Region	70 – 74	5	Substrate binding By similarity
	Region	195 – 196	2	Substrate binding By similarity
Sites
	Active site	133	1	Nucleophile
	Binding site	21	1	FMN By similarity
	Binding site	46	1	Substrate By similarity
	Binding site	130	1	FMN By similarity
	Binding site	130	1	Substrate By similarity
	Binding site	168	1	FMN By similarity
	Binding site	194	1	FMN; via carbonyl oxygen By similarity
	Binding site	220	1	FMN; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1G864 [UniParc]. Last modified June 27, 2006. Version 1. Checksum: 799B034239D6C885	FASTA	307	32,181
	10 20 30 40 50 60 MVNTHVNLPG LDLKNPVMPA SGTFGFGDVP AAQKFDLNDL GAMVIKTTTP HATTGNPQPQ 70 80 90 100 110 120 IAILEDGVLN SVGLTNPGVD QVISEKLTKL RHQYLDLPIM ASVGGDSEDD YVEVAKKLSA 130 140 150 160 170 180 SGLVNALEIN VSCPNVAQGG MSFGVHAGVV EELTKKIKMA VALPIYVKLT PNVTDIVEIA 190 200 210 220 230 240 KAAESGGADG ISMINTVLGM RIDVKTRKPL LGHNMGGLSG EAVKPIAIRM ISQVRQVTQL 250 260 270 280 290 300 PIIGMGGIST AQDVIEFILA GANAVAVGSA HFEDELAAKH IAENLPAELE KLGIEDINDL VGQVKFN

References

[1]

"The complete genome sequence of Lactobacillus bulgaricus reveals extensive and ongoing reductive evolution." van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P., Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R., Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P. , Weissenbach J., Ehrlich S.D., Maguin E. Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 11842 / DSM 20081.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR954253 Genomic DNA. Translation: CAI98852.1.
RefSeq	YP_619726.1. NC_008054.1.
3D structure databases
ProteinModelPortal	Q1G864.
ModBase	Search...
Protein-protein interaction databases
STRING	390333.Ldb2114.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAI98852; CAI98852; Ldb2114.
GeneID	4084395.
KEGG	ldb:Ldb2114.
PATRIC	22219615. VBILacDel123523_1862.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0167.
HOGENOM	HOG000225105.
KO	K00226.
OMA	PILANKT.
ProtClustDB	PRK07259.
Enzyme and pathway databases
BioCyc	LDEL390333:GIXG-2083-MONOMER.
UniPathway	UPA00070.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_00224. DHO_dh_type1.
InterPro	IPR013785. Aldolase_TIM. IPR005720. Dihydroorotate_DH. IPR024920. Dihydroorotate_DH_1. IPR012135. Dihydroorotate_DH_1_2. IPR001295. Dihydroorotate_DH_CS. [Graphical view]
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. False negative. PS00912. DHODEHASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRDA_LACDA

Accession

Primary (citable) accession number: Q1G864

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	June 27, 2006
Last modified:	May 1, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program