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A0JX31 (PYRD_ARTS2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydroorotate dehydrogenase (quinone)
EC=1.3.5.2
Alternative name(s):
DHOdehase
Short name=DHOD
Short name=DHODase
Dihydroorotate oxidase
Gene names
Name:pyrD
Ordered Locus Names:Arth_2221
OrganismArthrobacter sp. (strain FB24) [Complete proteome] [HAMAP]
Taxonomic identifier290399 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

Protein attributes

Sequence length357 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor By similarity. HAMAP MF_00225

Catalytic activity

(S)-dihydroorotate + a quinone = orotate + a quinol. HAMAP MF_00225

Cofactor

Binds 1 FMN per subunit By similarity. HAMAP MF_00225

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. HAMAP MF_00225

Subunit structure

Monomer By similarity. HAMAP MF_00225

Subcellular location

Cell membrane; Peripheral membrane protein By similarity HAMAP MF_00225.

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

   Cellular componentplasma membrane

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 – 357357Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
PRO_0000336453

Regions

Nucleotide binding67 – 715FMN By similarity
Nucleotide binding332 – 3332FMN By similarity
Region116 – 1205Substrate binding By similarity
Region257 – 2582Substrate binding By similarity

Sites

Active site1891Nucleophile By similarity
Binding site711Substrate By similarity
Binding site911FMN; via amide nitrogen By similarity
Binding site1531FMN By similarity
Binding site1861FMN By similarity
Binding site1861Substrate By similarity
Binding site1911Substrate By similarity
Binding site2281FMN By similarity
Binding site2561FMN; via carbonyl oxygen By similarity
Binding site2821FMN; via amide nitrogen By similarity
Binding site3111FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
A0JX31 [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."
US DOE Joint Genome Institute
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].
Strain: FB24.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000454 Genomic DNA. Translation: ABK03601.1.
RefSeqYP_831701.1. NC_008541.1.

3D structure databases

ProteinModelPortalA0JX31.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0JX31.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4445282.
GenomeReviewsGene locus Arth_2221 in contig CP000454_GR.
KEGGart:Arth_2221.
PATRIC20999783. VBIArtSp72239_2589.
TIGRArth_2221.

Phylogenomic databases

eggNOGCOG0167.
HOGENOMHBG351027.
OMAAALNRMG.
PhylomeDBA0JX31.
ProtClustDBPRK05286.

Enzyme and pathway databases

BioCycASP1667:ARTH_2221-MONOMER.

Family and domain databases

HAMAPMF_00225. DHO_dh_type2.
[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.
KOK00226.
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: January 25, 2012
This is version 43 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

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