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Reviewed, UniProtKB/Swiss-Prot A0JX31 (PYRD_ARTS2)

Last modified June 16, 2009. 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
    EC=1.3.3.1
Alternative name(s):
    Dihydroorotate oxidase
    DHOdehase
      Short name=DHODase
      Short name=DHOD
Gene names
Name: pyrD
Ordered Locus Names: Arth_2221
OrganismArthrobacter sp. (strain FB24) [Complete proteome] [HAMAP]
Taxonomic identifier290399 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

Protein attributes

Sequence length357 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + O2 = orotate + H2O2. HAMAP MF_00225

Cofactor

Binds 1 FMN per subunit By similarity.

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 4/6. HAMAP MF_00225

Subunit structure

Homodimer By similarity.

Subcellular location

Cell membrane; Peripheral membrane protein By similarity.

Sequence similarities

Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Cellular componentCell membrane
Membrane
   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 componentplasma membrane

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 – 357357Dihydroorotate dehydrogenase HAMAP MF_00225
PRO_0000336453

Sites

Active site1891Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
A0JX31-1 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: ABD678D314C22CB4

FASTA35738,147
        10         20         30         40         50         60 
MRVYPTFFRL AFSWMDAERA HRIGFRAIRL AHSSGAGRVL AKFTAPAPSL QTTAFGITFP 

        70         80         90        100        110        120 
SPFGLAAGFD KEGHGIEALT ELGFGHVEVG TITGQAQPGN EKPRLFRLVE DKAVINRMGF 

       130        140        150        160        170        180 
NNDGATAVAP RLKSARAALQ RRHPGVRPVI GVNIGKSKVV ELEDAASDYL VSARSLAPAA 

       190        200        210        220        230        240 
DYLVVNVSSP NTPGLRLLQN VETLRPLLKA VGEEADKAAG RHVPLLVKIA PDLTDEDIDD 

       250        260        270        280        290        300 
VAKLALDLGL DGIIATNTTI GREGLTSDPE KIRDCGPGGL SGAPLKARSL EVLRRLKEAT 

       310        320        330        340        350 
GGSLTLVSVG GVENARDVQE RLDAGATLVQ GYTAFLYEGP FWAARINRQL AKHPARR 

« Hide

References

[1]"Complete sequence of chromosome 1 of Arthrobacter sp. FB24."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Thompson S., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K., Nakatsu C.H., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000454 Genomic DNA. Translation: ABK03601.1.
RefSeqYP_831701.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4445282.
GenomeReviewsGene locus Arth_2221 in contig CP000454_GR.
KEGGart:Arth_2221.
TIGRArth_2221.

Phylogenomic databases

OMAA0JX31. AALNRMG.

Family and domain databases

HAMAPMF_00225.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005719. Dihydroorotate_DH_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.
TIGRFAMsTIGR01036. pyrD_sub2. 1 hit.
PROSITEPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRD_ARTS2
AccessionPrimary (citable) accession number: A0JX31
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: December 12, 2006
Last modified: June 16, 2009
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