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UniProtKB/Swiss-Prot entry Q8K9L2

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

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Entry information
Entry name PYRC_BUCAP
Primary accession number Q8K9L2
Secondary accession numbers None
Integrated into Swiss-Prot on November 8, 2002
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 46)
Name and origin of the protein
Protein name Dihydroorotase
Synonyms DHOase
EC 3.5.2.3
Gene name
Name: pyrC
OrderedLocusNames: BUsg_322
From
Buchnera aphidicola subsp. Schizaphis graminum [TaxID: 98794] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1071278; PubMed=12089438 [NCBI, ExPASy, EBI, Israel, Japan]
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
"50 million years of genomic stasis in endosymbiotic bacteria.";
Science 296:2376-2379(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
AE013218; AAM67876.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_660665.1; -.
3D structure databases
HSSP P05020; 1J79. [HSSP ENTRY / PDB]
ModBase Q8K9L2.
Enzyme and pathway databases
BioCyc BAPH198804:BUSG322-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 Q8K9L2.
Genome annotation databases
GeneID 1005527; -.
GenomeReviews AE013218_GR; BUsg_322.
KEGG bas:BUsg322; -.
Phylogenomic databases
HOGENOM Q8K9L2; -.
Genome annotation databases
CMR Q8K9L2; BUsg_322.
Other
ProtoNet Q8K9L2.
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   349  349     Dihydroorotase. PRO_0000147204
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   252   252        Zinc 1 (By similarity). 
MOD_RES   103   103        N6-carboxylysine (By similarity). 
Sequence information
Length: 349 AA [This is the length of the unprocessed precursor] Molecular weight: 40557 Da [This is the MW of the unprocessed precursor] CRC64: 03D6ADFD7BCE0BC5 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSKFLKKIKI IKPDDWHVHL RDNEILKKVS QYTGTFYKRA IIMPNLEEPI TNCFRSISYR 

        70         80         90        100        110        120 
RRILNSMTPN TAFQPLMICY LTEKTSPEEL QQGFFKKIFV GAKLYPHCST TNSKYGIKNI 

       130        140        150        160        170        180 
NNIYHLFNIM EKIKMPLLIH GEENNLNIDI YDREAKFIEN TLKPLRKKFP ELKIILEHIT 

       190        200        210        220        230        240 
TEEAISYIEE CNSSYLAGTI TPHHLMLNRN NMFIDGIQPH LYCLPLLKRK KHQIALRNVI 

       250        260        270        280        290        300 
SSGSKNFFLG SDTAPHFHKN KINTFGCAGI FNAPSSLLCY VSVFEEMNAL QHFQSFCSEN 

       310        320        330        340 
GPNFYNMPIN KETITLVKKP HKILEKINIG KNIIVPFLAG KRLDWSIEK
Q8K9L2 in FASTA format

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