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 A0RHR0

[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 PYRC_BACAH
Primary accession number A0RHR0
Secondary accession numbers None
Integrated into Swiss-Prot on March 18, 2008
Sequence was last modified on January 9, 2007 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 17)
Name and origin of the protein
Protein name Dihydroorotase
Synonyms DHOase
EC 3.5.2.3
Gene name
Name: pyrC
OrderedLocusNames: BALH_3518
From
Bacillus thuringiensis (strain Al Hakam) [TaxID: 412694] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus cereus group.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.00241-07; PubMed=17337577 [NCBI, ExPASy, EBI, Israel, Japan]
Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.;
"The complete genome sequence of Bacillus thuringiensis Al Hakam.";
J. Bacteriol. 189:3680-3681(2007).
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
CP000485; ABK86753.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_896260.1; -.
3D structure databases
ModBase A0RHR0.
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; 1.
PS00483; DIHYDROOROTASE_2; 1.
BLOCKS A0RHR0.
ProtoNet A0RHR0.
Genome annotation databases
GeneID 4544126; -.
GenomeReviews CP000485_GR; BALH_3518.
KEGG btl:BALH_3518; -.
CMR A0RHR0; BALH_3518.
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   428  428     Dihydroorotase. PRO_0000325588
METAL   59    59        Zinc 1 (By similarity). 
METAL   61    61        Zinc 1 (By similarity). 
METAL   141   141        Zinc 1; via carbamate group (By similarity). 
METAL   141   141        Zinc 2; via carbamate group (By similarity). 
METAL   178   178        Zinc 2 (By similarity). 
METAL   231   231        Zinc 2 (By similarity). 
METAL   304   304        Zinc 1 (By similarity). 
MOD_RES   141   141        N6-carboxylysine (By similarity). 
Sequence information
Length: 428 AA [This is the length of the unprocessed precursor] Molecular weight: 46598 Da [This is the MW of the unprocessed precursor] CRC64: 7769493E6B0ED093 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MNYLFKNGRY MNEEGKIVAT DLLVQDGKIA KVAENITADN AEVIDVNGKL IAPGLVDVHV 

        70         80         90        100        110        120 
HLREPGGEHK ETIETGTLAA AKGGFTTICA MPNTRPVPDC REHMEDLQNR IKEKAHVNVL 

       130        140        150        160        170        180 
PYGAITVRQA GSEMTDFETL KELGAFAFTD DGVGVQDASM MLAAMKRAAK LNMAVVAHCE 

       190        200        210        220        230        240 
ENTLINKGCV HEGKFSEKHG LNGIPSVCES VHIARDILLA EAADCHYHVC HVSTKGSVRV 

       250        260        270        280        290        300 
IRDAKRAGIK VTAEVTPHHL VLCEDDIPSA DPNFKMNPPL RGKEDHAALI EGLLDGTIDM 

       310        320        330        340        350        360 
IATDHAPHTA EEKAQGIERA PFGITGFETA FPLLYTNLVK KGIITLEQLI QFLTEKPADT 

       370        380        390        400        410        420 
FGLEAGRLKE GRTADITIID LEQEEEIDPT TFLSKGKNTP FAGWKCQGWP VMTIVGGKIA 


WQKESALV
A0RHR0 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 ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!