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UniProtKB/Swiss-Prot entry A3N925

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PYRD_BURP6
Primary accession number A3N925
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on April 3, 2007 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 17)
Name and origin of the protein
Protein name Dihydroorotate dehydrogenase
Synonyms EC 1.3.3.1
Dihydroorotate oxidase
DHOdehase
DHODase
DHOD
Gene name
Name: pyrD
OrderedLocusNames: BURPS668_1809
From
Burkholderia pseudomallei (strain 668) [TaxID: 320373] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei group.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DeShazer D., Woods D.E., Nierman W.C.;
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CP000570; ABN82176.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001058846.1; -.
3D structure databases
ModBase A3N925.
Ontologies
GO
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from HAMAP).
GO:0004158; Molecular function: dihydroorotate oxidase activity (inferred from electronic annotation from HAMAP).
GO:0006207; Biological process: 'de novo' pyrimidine base biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006222; Biological process: UMP biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
HAMAP MF_00225; -; 1.
PBIL [Tree]
InterPro IPR013785; Aldolase_TIM.
IPR012135; DHO_DHase_1_2.
IPR005719; DHO_DHase_2.
IPR001295; Dihydroorotate_DHase_core.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
Pfam PF01180; DHO_dh; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000164; DHO_oxidase; 1.
TIGRFAMs TIGR01036; pyrD_sub2; 1.
PROSITE PS00911; DHODEHASE_1; 1.
PS00912; DHODEHASE_2; 1.
ProtoNet A3N925.
Genome annotation databases
GeneID 4881949; -.
GenomeReviews CP000570_GR; BURPS668_1809.
KEGG bpd:BURPS668_1809; -.
NMPDR fig|320373.3.peg.2587; -.
TIGR BURPS668_1809; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell membrane; Complete proteome; Flavoprotein; FMN; Membrane; Oxidoreductase; Pyrimidine biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   342  342     Dihydroorotate dehydrogenase. PRO_1000024163
ACT_SITE   178   178        Nucleophile (By similarity). 
Sequence information
Length: 342 AA [This is the length of the unprocessed precursor] Molecular weight: 36305 Da [This is the MW of the unprocessed precursor] CRC64: 5E7244A6476813E7 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MFSSLYPLAR ASLFKMDAED AHHLTLRMLG AAGRTGLACA LSPRVPDAPR TVMGLSFRNP 

        70         80         90        100        110        120 
VGLAAGLDKD GAAIDGFAAL GFGFIEVGTV TPRAQPGNPR PRLFRLPEAD AIINRMGFNN 

       130        140        150        160        170        180 
SGVDQFVKNV QAARYRGVLG LNIGKNADTP IERAADDYLY CLERVYPFAS YVTINISSPN 

       190        200        210        220        230        240 
TKNLRQLQGA GELDALLAAL KDKQRRLADL HGKLVPLALK IAPDLDDEQV KEIAATLLRH 

       250        260        270        280        290        300 
DIEGVIATNT TLSREAVKGL PHADEAGGLS GRPVFDASNA VIRKLRAELG DAVPIIGVGG 

       310        320        330        340 
IFSGEDARAK LAAGAALVQL YTGFIYRGPA LVAECVKAIA RG
A3N925 in FASTA format

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