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UniProtKB/Swiss-Prot entry Q1WVB1

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

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Entry information
Entry name PYRC_LACS1
Primary accession number Q1WVB1
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on May 2, 2006 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 18)
Name and origin of the protein
Protein name Dihydroorotase
Synonyms DHOase
EC 3.5.2.3
Gene name
Name: pyrC
OrderedLocusNames: LSL_0191
From
Lactobacillus salivarius subsp. salivarius (strain UCC118) [TaxID: 362948] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae; Lactobacillus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0511060103; PubMed=16617113 [NCBI, ExPASy, EBI, Israel, Japan]
Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P., Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K., Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
"Multireplicon genome architecture of Lactobacillus salivarius.";
Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(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
CP000233; ABD99006.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_535089.1; -.
3D structure databases
ModBase Q1WVB1.
Protein family/group databases
MEROPS M38.972; -.
Enzyme and pathway databases
BioCyc LSAL362948:LSL_0191-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_00220; -; 1.
PBIL [Tree]
InterPro IPR006680; Amidohydro_1.
IPR004722; DHOmult.
IPR002195; Dihydroorotase_CS.
Graphical view of domain structure.
Pfam PF01979; Amidohydro_1; 1.
Pfam graphical view of domain structure.
ProDom PD000518; DHOase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00857; pyrC_multi; 1.
PROSITE PS00482; DIHYDROOROTASE_1; FALSE_NEG.
PS00483; DIHYDROOROTASE_2; 1.
BLOCKS Q1WVB1.
Genome annotation databases
GeneID 3978041; -.
GenomeReviews CP000233_GR; LSL_0191.
KEGG lsl:LSL_0191; -.
Phylogenomic databases
HOGENOM Q1WVB1; -.
Genome annotation databases
CMR Q1WVB1; LSL_0191.
Other
ProtoNet Q1WVB1.
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   429  429     Dihydroorotase. PRO_1000024091
METAL   61    61        Zinc 1 (By similarity). 
METAL   63    63        Zinc 1 (By similarity). 
METAL   143   143        Zinc 1 (via carbamate group) (By similarity). 
METAL   143   143        Zinc 2 (via carbamate group) (By similarity). 
METAL   180   180        Zinc 2 (By similarity). 
METAL   233   233        Zinc 2 (By similarity). 
METAL   306   306        Zinc 1 (By similarity). 
MOD_RES   143   143        N6-carboxylysine (By similarity). 
Sequence information
Length: 429 AA [This is the length of the unprocessed precursor] Molecular weight: 46735 Da [This is the MW of the unprocessed precursor] CRC64: 7A32DF5D16BE2303 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MATLIKNGNL YQAGRIYQAD VLIEDGKIKA IGKNLSDVVK ENLVEIDATN KLVAPGLVDV 

        70         80         90        100        110        120 
HVHYRDPGFT YKETIHTGSL AAAHGGYTTV CAMPNLDPVP DTPELVEKMC SRNQEDGVVK 

       130        140        150        160        170        180 
VKQYGSITHG LKSEELVDFV GMKKAGAFAF SNDGSGVQTA GTMYQAMKSA AALNMAIVAH 

       190        200        210        220        230        240 
VEDNSLLFGG VMNAGKRADE LGLPGILGIS ESSQIARDLL LAKETGVHYH VCHVSTKESV 

       250        260        270        280        290        300 
ELVRLAKQHK INVTCEVSPH HLLLADVDIP GNDPYYKMNP PLRGVEDRQA LIDSLLDGTI 

       310        320        330        340        350        360 
DMIATDHAPH SIDEKTGDMR EASFGITGSE TAFAMLYTKF VKTGIFTLEQ LLQWMSINPA 

       370        380        390        400        410        420 
EKFGMEDAGE LLPGKSADLA IFDLNKEYVI KEEDYLSKGI NTPFTGEKVY GQTVLTMVDG 


QKVYQREEK
Q1WVB1 in FASTA format

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