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UniProtKB/Swiss-Prot entry Q8FIR2

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

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Entry information
Entry name PYRC_ECOL6
Primary accession number Q8FIR2
Secondary accession numbers None
Integrated into Swiss-Prot on August 22, 2003
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 43)
Name and origin of the protein
Protein name Dihydroorotase
Synonyms DHOase
EC 3.5.2.3
Gene name
Name: pyrC
OrderedLocusNames: c1329
From
Escherichia coli O6 [TaxID: 217992] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
DOI=10.1073/pnas.252529799; PubMed=12471157 [NCBI, ExPASy, EBI, Israel, Japan]
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(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
AE014075; AAN79802.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_753242.1; -.
3D structure databases
HSSP P05020; 1J79. [HSSP ENTRY / PDB]
ModBase Q8FIR2.
Ontologies
GO
GO:0004151; Molecular function: dihydroorotase activity (inferred from electronic annotation from HAMAP).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from HAMAP).
GO:0006221; Biological process: pyrimidine nucleotide biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00219; -; 1.
PBIL [Tree]
InterPro IPR006680; Amidohydro_1.
IPR004721; DHOdimr.
IPR002195; Dihydroorotase_CS.
Graphical view of domain structure.
Pfam PF01979; Amidohydro_1; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001237; DHOdimr; 1.
TIGRFAMs TIGR00856; pyrC_dimer; 1.
PROSITE PS00482; DIHYDROOROTASE_1; 1.
PS00483; DIHYDROOROTASE_2; 1.
BLOCKS Q8FIR2.
Genome annotation databases
GeneID 1035029; -.
GenomeReviews AE014075_GR; c1329.
KEGG ecc:c1329; -.
NMPDR fig|199310.1.peg.1285; -.
Phylogenomic databases
HOGENOM Q8FIR2; -.
Genome annotation databases
CMR Q8FIR2; c1329.
Other
ProtoNet Q8FIR2.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Hydrolase; Metal-binding; Pyrimidine biosynthesis; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   348  347     Dihydroorotase. PRO_0000147206
METAL   17    17        Zinc 1 (By similarity). 
METAL   19    19        Zinc 1 (By similarity). 
METAL   103   103        Zinc 1; via carbamate group (By similarity). 
METAL   103   103        Zinc 2; via carbamate group (By similarity). 
METAL   140   140        Zinc 2 (By similarity). 
METAL   178   178        Zinc 2 (By similarity). 
METAL   251   251        Zinc 1 (By similarity). 
MOD_RES   103   103        N6-carboxylysine (By similarity). 
Sequence information
Length: 348 AA [This is the length of the unprocessed precursor] Molecular weight: 38760 Da [This is the MW of the unprocessed precursor] CRC64: 693414ADEEE3646D [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTAPSQVLKI RCPDDWHLHL RDGDMLKTVV PYTSEIYGRA IVMPNLAPPV TTVEAAVAYR 

        70         80         90        100        110        120 
QRILDAVPAG HDFTPLMTCY LTDSLDPNEL ERGFNEGVFT AAKLYPANAT TNSSHGVTSV 

       130        140        150        160        170        180 
DAIMPVLERM EKIGMPLLVH GEVTHADIDI FDREARFIES VMEPLRQRLT ALKVVFEHIT 

       190        200        210        220        230        240 
TKDAADYVRD GNERLAATIT PQHLMFNRNH MLVGGVRPHL YCLPILKRNI HQQALRELVA 

       250        260        270        280        290        300 
SGFNRVFLGT DSAPHARHRK ESSCGCAGCF NAPTALGSYA TVFEEMNALQ HFEAFCSVNG 

       310        320        330        340 
PQFYGLPVND TFIELVREEQ QVAESIALTD DTLVPFLAGE TVRWSVKQ
Q8FIR2 in FASTA format

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