ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q8K9I5

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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PYRD_BUCAP
Primary accession number Q8K9I5
Secondary accession numbers None
Integrated into Swiss-Prot on November 8, 2002
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 51)
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: BUsg_350
From
Buchnera aphidicola subsp. Schizaphis graminum [TaxID: 98794] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1071278; PubMed=12089438 [NCBI, ExPASy, EBI, Israel, Japan]
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
"50 million years of genomic stasis in endosymbiotic bacteria.";
Science 296:2376-2379(2002).
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
AE013218; AAM67903.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_660692.1; -.
3D structure databases
HSSP P05021; 1F76. [HSSP ENTRY / PDB]
ModBase Q8K9I5.
Enzyme and pathway databases
BioCyc BAPH198804:BUSG350-MON; -.
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.
Genome annotation databases
GeneID 1005806; -.
GenomeReviews AE013218_GR; BUsg_350.
KEGG bas:BUsg350; -.
Phylogenomic databases
HOGENOM Q8K9I5; -.
Genome annotation databases
CMR Q8K9I5; BUsg_350.
Other
ProtoNet Q8K9I5.
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   336  336     Dihydroorotate dehydrogenase. PRO_0000148427
ACT_SITE   175   175        Nucleophile (By similarity). 
Sequence information
Length: 336 AA [This is the length of the unprocessed precursor] Molecular weight: 38101 Da [This is the MW of the unprocessed precursor] CRC64: 19B8F807BF49DE83 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MFYYLIRKLL FLIDPEKAHT LVLMYLNSKK IQILRKIFIK PIPLKQIKCM GLTFNNKIGL 

        70         80         90        100        110        120 
AAGMDKNGDY IDSLSKIGFG FIEVGTVTPL PQYGNPKPRI FRVPSIEGII NRMGFNNLGI 

       130        140        150        160        170        180 
DYLVNNVKKS KFKGIIGINI GKNKDTKIED AIKDYLICIE KIYFYASYIA INISSPNTIN 

       190        200        210        220        230        240 
LRKLQYGILF ENLLRDIKKK QSEMHSKYSK YVPIVIKISP DLSKKELIHI SNKLIHYKID 

       250        260        270        280        290        300 
GVIATNTTLD HSSIPKIKNN KEEGGLSGLP LQKKSNDVIS ILYKNLKRKI PIIGVGGINS 

       310        320        330 
INSAREKIMC GANLIQVYSG LIYHGPNFIR EIIRNL
Q8K9I5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ca flag CBR Canada Mirror sites: Australia Brazil China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!