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UniProtKB/Swiss-Prot entry Q1RD95

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

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Entry information
Entry name PYRC_ECOUT
Primary accession number Q1RD95
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on May 16, 2006 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 19)
Name and origin of the protein
Protein name Dihydroorotase
Synonyms DHOase
EC 3.5.2.3
Gene name
Name: pyrC
OrderedLocusNames: UTI89_C1187
From
Escherichia coli (strain UTI89 / UPEC) [TaxID: 364106] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0600938103; PubMed=16585510 [NCBI, ExPASy, EBI, Israel, Japan]
Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I.;
"Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach.";
Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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
CP000243; ABE06669.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_540200.1; -.
3D structure databases
SMR Q1RD95; 5-347.
ModBase Q1RD95.
Enzyme and pathway databases
BioCyc ECOL364106:UTI89_C1187-MON; -.
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 Q1RD95.
ProtoNet Q1RD95.
Genome annotation databases
GeneID 3994733; -.
GenomeReviews CP000243_GR; UTI89_C1187.
KEGG eci:UTI89_C1187; -.
Phylogenomic databases
HOGENOM Q1RD95; -.
Genome annotation databases
CMR Q1RD95; UTI89_C1187.
Other
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
CHAIN   1   348  348     Dihydroorotase. PRO_1000024011
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: 38839 Da [This is the MW of the unprocessed precursor] CRC64: 2EEFB26B323419A0 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTAPSQVLKI RRPDDWHLHL 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 YFEAFCSVNG 

       310        320        330        340 
PQFYGLPVND TFIELVREEQ QVAESIALTD DTLVPFLAGE TVRWSVKQ
Q1RD95 in FASTA format

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