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Reviewed, UniProtKB/Swiss-Prot Q7NX17 (PYRD_CHRVO)

Last modified June 16, 2009. Version 48. 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: CV_1812
OrganismChromobacterium violaceum [Complete proteome] [HAMAP]
Taxonomic identifier536 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeChromobacterium

Protein attributes

Sequence length344 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 – 344344Dihydroorotate dehydrogenase HAMAP MF_00225
PRO_0000148430

Sites

Active site1751Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NX17-1 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: B82DF4DADE8FCB65

FASTA34436,843
        10         20         30         40         50         60 
MLYPLLRPLL FKFDAETAHE HTLKMLDRAH RLHLTPLAAS PAARQPVQAM GLTFPNPVGL 

        70         80         90        100        110        120 
AAGLDKNGAH IDALAALGFG FIEIGTVTPR PQDGNPKPRL FRLPEHEAII NRMGFNNHGV 

       130        140        150        160        170        180 
AALLDNVRRS KFKGVLGINI GKNAITPIEN AVDDYLACLD QVYAAASYVT VNISSPNTKN 

       190        200        210        220        230        240 
LRQLQQGDEL GRLLAALKQR QLALADQHGR YVPLAVKIAP DLDDEQIAEI ARLLTGNGID 

       250        260        270        280        290        300 
GVIATNTTLS RREVAGHPLE SEAGGLSGAP VRARSTEVIR KLHKELGGAM PIIGVGGILS 

       310        320        330        340 
GNDAVEKLDA GASLVQLYSG LIYRGPELVG ECARATAQYL QARN 

« Hide

References

[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131.

Cross-references

Sequence databases

AE016825 Genomic DNA. Translation: AAQ59486.1.
RefSeqNP_901482.1.

3D structure databases

HSSPHSSP built from PDB template 1F76 based on UniProtKB P05021.
ModBaseSearch...

Genome annotation databases

GeneID2550125.
GenomeReviewsGene locus CV_1812 in contig AE016825_GR.
KEGGcvi:CV_1812.
NMPDRfig|243365.1.peg.1812.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ7NX17.
OMAQ7NX17. NAEQQGG.

Enzyme and pathway databases

BioCycCVIO243365:CV_1812-MON.
BRENDA1.3.3.1. 415.

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_CHRVO
AccessionPrimary (citable) accession number: Q7NX17
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: December 15, 2003
Last modified: June 16, 2009
This is version 48 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