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Reviewed, UniProtKB/Swiss-Prot A2RJT9 (PYRDA_LACLM)

Last modified February 9, 2010. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dihydroorotate dehydrogenase A
    EC=1.3.3.1
Alternative name(s):
    Dihydroorotate oxidase A
    DHOdehase A
      Short name=DHODase A
      Short name=DHOD A
Gene names
Name: pyrDA
Ordered Locus Names: llmg_0952
OrganismLactococcus lactis subsp. cremoris (strain MG1363) [Complete proteome] [HAMAP]
Taxonomic identifier416870 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeLactococcus

Protein attributes

Sequence length311 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + O2 = orotate + H2O2. HAMAP MF_00224

Cofactor

Binds 1 FMN per subunit By similarity. HAMAP MF_00224

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (O2 route): step 1/1. HAMAP MF_00224

Subunit structure

Homodimer By similarity. HAMAP MF_00224

Subcellular location

Cytoplasm By similarity HAMAP MF_00224.

Miscellaneous

Can use fumarate but not NAD as an electron acceptor. HAMAP MF_00224

Sequence similarities

Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Cellular componentCytoplasm
   LigandFMN
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete 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 componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondihydroorotate oxidase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 311311Dihydroorotate dehydrogenase A HAMAP MF_00224
PRO_0000285239

Sites

Active site1301Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
A2RJT9-1 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: 30157E3C2791CDD7

FASTA31134,210
        10         20         30         40         50         60 
MLNTTFANAK FANPFMNASG VHCMTIEDLE ELKASQAGAY ITKSSTLEKR EGNPLPRYVD 

        70         80         90        100        110        120 
LELGSINSMG LPNLGFDYYL DYVLKNQKEN AQEGPIFFSI AGMSAAENIA MLKKIQESDF 

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

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

       250        260        270        280        290        300 
PEIQIIGTGG IETGQDAFEH LLCGATMLQI GTALHKEGPA IFDRIIKELE EIMNQKGYQS 

       310 
IADFHGKLKS L 

« Hide

References

« Hide 'large scale' references
[1]"Two different dihydroorotate dehydrogenases in Lactococcus lactis."
Andersen P.S., Jansen P.J.G., Hammer K.
J. Bacteriol. 176:3975-3982(1994) [PubMed: 8021180] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete genome sequence of the lactic acid bacterial paradigm Lactococcus lactis subsp. cremoris MG1363."
Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C., Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P., van Sinderen D., Kok J.
J. Bacteriol. 189:3256-3270(2007) [PubMed: 17307855] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X74206 Genomic DNA. Translation: CAA52279.1.
AM406671 Genomic DNA. Translation: CAL97544.1.
RefSeqYP_001032274.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA2RJT9.

Genome annotation databases

GeneID4798428.
GenomeReviewsGene locus llmg_0952 in contig AM406671_GR.
KEGGllm:llmg_0952.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0167.
HOGENOMHBG472415.
OMAKPLGVKL.

Family and domain databases

HAMAPMF_00224_B. DHO_dh_type1_B.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005720. Dihydroorotate_DH_1_core.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
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_LACLM
AccessionPrimary (citable) accession number: A2RJT9
Secondary accession number(s): P54321
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: March 6, 2007
Last modified: February 9, 2010
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents