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Q53ZE5 (PYRDA_LACLC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. 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
OrganismLactococcus lactis subsp. cremoris (Streptococcus cremoris)
Taxonomic identifier1359 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeLactococcus

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 MF_00224

Catalytic activity

(S)-dihydroorotate + fumarate = orotate + succinate. HAMAP MF_00224

Cofactor

Binds 1 FMN per subunit By similarity. HAMAP MF_00224

Pathway

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

Subunit structure

Homodimer By similarity. HAMAP MF_00224

Subcellular location

Cytoplasm By similarity 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
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

   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 MF_00224
PRO_0000148394

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
Q53ZE5 [UniParc].

Last modified May 24, 2005. 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

[1]"Lactococcus lactis subsp. cremoris gene encoding the biosynthetic enzyme dihydroorotate dehydrogenase family 1a."
Hall C.R., Dietrich F.S.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NCK436.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY323899 Genomic DNA. Translation: AAQ01776.1.

3D structure databases

ProteinModelPortalQ53ZE5.
SMRQ53ZE5. Positions 1-311.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_00224. DHO_dh_type1.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR005720. Dihydroorotate_DH.
IPR024920. Dihydroorotate_DH_1.
IPR012135. Dihydroorotate_DH_1_2.
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_LACLC
AccessionPrimary (citable) accession number: Q53ZE5
Secondary accession number(s): P54321
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 24, 2005
Last modified: January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families