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A6VP48 (PYRD_ACTSZ) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 36. 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:Asuc_1385
OrganismActinobacillus succinogenes (strain ATCC 55618 / 130Z) [Complete proteome] [HAMAP]
Taxonomic identifier339671 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus

Protein attributes

Sequence length340 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 – 340340Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
PRO_1000071764

Regions

Nucleotide binding65 – 695FMN By similarity
Nucleotide binding321 – 3222FMN By similarity
Region114 – 1185Substrate binding By similarity
Region249 – 2502Substrate binding By similarity

Sites

Active site1781Nucleophile By similarity
Binding site691Substrate By similarity
Binding site891FMN; via amide nitrogen By similarity
Binding site1421FMN By similarity
Binding site1751FMN By similarity
Binding site1751Substrate By similarity
Binding site1801Substrate By similarity
Binding site2201FMN By similarity
Binding site2481FMN; via carbonyl oxygen By similarity
Binding site2711FMN; via amide nitrogen By similarity
Binding site3001FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
A6VP48 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 887C5F00632C2B96

FASTA34037,055
        10         20         30         40         50         60 
MLYPLIRKGI FALEPETAHN LAIKALHIAG NPWLNRALKA LLGCPQGTEK TVMGIKFKNP 

        70         80         90        100        110        120 
IGLAAGADKN GEAIDGFGAM GFGFIEVGTV TPLAQDGNAK PRQFRIVEAE GIINRNGFNN 

       130        140        150        160        170        180 
YGIDHLIENV NKSHYDGTLG INIGKNKITP IEQGKDDYIF CLNKAYNYAH YITVNISSPN 

       190        200        210        220        230        240 
TPDLRTLQYG DALDDLLKSI KERQKILAEQ YNKYVPIALK IAPDLTEAEL VQIADTVRRH 

       250        260        270        280        290        300 
QMDGVIATNT TISRDTVQGM KNAAEIGGLS GKPLQHKSTE IIRRLHRELK GDIPIIGSGG 

       310        320        330        340 
IDGVQNAQEK IAAGAELLQI YSGLIYHGPA LVKTLVQTIK

« Hide

References

[1]"Complete sequence of Actinobacillus succinogenes 130Z."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Vieille C., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 55618 / 130Z.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000746 Genomic DNA. Translation: ABR74745.1.
RefSeqYP_001344680.1. NC_009655.1.

3D structure databases

ProteinModelPortalA6VP48.
SMRA6VP48. Positions 1-339.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6VP48.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5348572.
GenomeReviewsGene locus Asuc_1385 in contig CP000746_GR.
KEGGasu:Asuc_1385.
PATRIC20761144. VBIActSuc117883_1448.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0167.
HOGENOMHBG351027.
OMASYVTVNI.
ProtClustDBPRK05286.

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_ACTSZ
AccessionPrimary (citable) accession number: A6VP48
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: August 21, 2007
Last modified: December 14, 2011
This is version 36 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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