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 A1TPZ2


[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_ACIAC
Primary accession number A1TPZ2
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on February 6, 2007 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 18)
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: Aave_2455
From
Acidovorax avenae subsp. citrulli (strain AAC00-1) [TaxID: 397945] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Comamonadaceae; Acidovorax.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
Submitted (DEC-2006) 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
CP000512; ABM33030.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_970804.1; -.
3D structure databases
ModBase A1TPZ2.
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).
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.
BLOCKS A1TPZ2.
Genome annotation databases
GeneID 4669515; -.
GenomeReviews CP000512_GR; Aave_2455.
KEGG aav:Aave_2455; -.
NMPDR fig|397945.5.peg.2100; -.
CMR A1TPZ2; Aave_2455.
Other
ProtoNet A1TPZ2.
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   359  359     Dihydroorotate dehydrogenase. PRO_1000024144
ACT_SITE   185   185        Nucleophile (By similarity). 
Sequence information
Length: 359 AA [This is the length of the unprocessed precursor] Molecular weight: 38731 Da [This is the MW of the unprocessed precursor] CRC64: E9B4DB527CFC5783 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSLIPYALTR PFLFGMDAEA AHELTMDMLA RGQRTPLQWA WSGEQVSDPV QLAGLTFPNR 

        70         80         90        100        110        120 
VGMAAGLDKN ARCIDALGAM GFGFVEVGTV TPRAQPGNPK PRMFRLPEAN ALINRLGFNN 

       130        140        150        160        170        180 
EGLDAFLHNV RQSNHHARPG MRPMLLGLNI GKNATTPIED ATRDYLLCLE GVYPHADYVT 

       190        200        210        220        230        240 
VNISSPNTQN LRALQSDAAL DGLLGAIAER RESLARQPEK ATGRPRRVPI FVKIAPDLAE 

       250        260        270        280        290        300 
EQVAVIASTL QRHGMDGVIA TNTTISRDAV QGLRHAEETG GLSGAPVREA SNRVIRQLRH 

       310        320        330        340        350 
ALGKDFPIIG VGGILSAEDA VEKIRAGADV VQIYTGLIYR GPALVPQVAK ALRAMPRPA 

A1TPZ2 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 kr flag YPRC Korea Mirror sites: Australia  Brazil  Canada  China  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!