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Q9CFC9 (PYRDA_LACLA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:pyrDA
Synonyms:pydA
Ordered Locus Names:LL1552
ORF Names:L192589
OrganismLactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis) [Reference proteome] [HAMAP]
Taxonomic identifier272623 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus

Protein attributes

Sequence length311 AA.
Sequence statusComplete.
Protein existenceInferred 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. HAMAP-Rule MF_00224

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway. HAMAP-Rule MF_00224

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00224

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00224.

Sequence similarities

Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Cellular componentCytoplasm
   LigandFlavoprotein
FMN
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   UncategorizedOBSOLETE:dihydroorotate oxidase (fumarate) activity

Inferred from electronic annotation. Source: UniProtKB-EC

   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_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondihydroorotate oxidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 311311Dihydroorotate dehydrogenase A (fumarate) HAMAP-Rule MF_00224
PRO_0000148393

Regions

Nucleotide binding43 – 442FMN By similarity
Nucleotide binding249 – 2502FMN By similarity
Nucleotide binding271 – 2722FMN By similarity
Region67 – 715Substrate binding By similarity
Region193 – 1942Substrate binding By similarity

Sites

Active site1301Nucleophile
Binding site191FMN By similarity
Binding site431Substrate By similarity
Binding site1271FMN By similarity
Binding site1271Substrate By similarity
Binding site1641FMN By similarity
Binding site1921FMN; via carbonyl oxygen By similarity
Binding site2211FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CFC9 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 80B3619EC408BBA8

FASTA31134,231
        10         20         30         40         50         60 
MLKTTFANAE FANPFMNASG VHCMTTEDLE ELKASQAGAY ITKSSTLEKR EGNPLPRYVD 

        70         80         90        100        110        120 
LELGSINSMG LPNLGFDYYL DYVLKNQKEK AQEAPIFFSI AGMSAAENIA MLKKIQESNF 

       130        140        150        160        170        180 
SGITELNLSC PNVPGKPQLA YDFEATEKLL KEVFTFFTKP LGVKLPPYFD LVHFDIMAEI 

       190        200        210        220        230        240 
LNQFPLTYVN SVNSIGNGLF IDSEAESVVI KPKDGFGGIG GAYIKPTALA NVRAFYTRLK 

       250        260        270        280        290        300 
PEIKIIGTGG IETGQDAFEH LLCGATMLQI GTALHKEGPA IFDRIIKELE EIMDKKGYQS 

       310 
IADFHGKLKS L 

« Hide

References

[1]"The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403."
Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J., Ehrlich S.D., Sorokin A.
Genome Res. 11:731-753(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IL1403.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005176 Genomic DNA. Translation: AAK05650.1.
PIRH86818.
RefSeqNP_267708.1. NC_002662.1.

3D structure databases

ProteinModelPortalQ9CFC9.
SMRQ9CFC9. Positions 1-311.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272623.L192589.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK05650; AAK05650; L192589.
GeneID1115211.
KEGGlla:L192589.
PATRIC22295518. VBILacLac136773_1666.

Phylogenomic databases

eggNOGCOG0167.
HOGENOMHOG000225104.
KOK00226.
OMADFDNCLM.
OrthoDBEOG6NPM9S.

Enzyme and pathway databases

BioCycLLAC272623:GHSH-1651-MONOMER.
SABIO-RKQ9CFC9.
UniPathwayUPA00070.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00224. DHO_dh_type1.
InterProIPR013785. Aldolase_TIM.
IPR005720. Dihydroorotate_DH.
IPR024920. Dihydroorotate_DH_1.
IPR012135. Dihydroorotate_DH_1_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
PfamPF01180. DHO_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMsTIGR01037. pyrD_sub1_fam. 1 hit.
PROSITEPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRDA_LACLA
AccessionPrimary (citable) accession number: Q9CFC9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: June 1, 2001
Last modified: May 14, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways