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 A1WC79

[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_ACISJ
Primary accession number A1WC79
Secondary accession numbers None
Integrated into Swiss-Prot on March 18, 2008
Sequence was last modified on February 6, 2007 (Sequence version 1)
Annotations were last modified on    September 2, 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: Ajs_3745
From
Acidovorax sp. (strain JS42) [TaxID: 232721] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Comamonadaceae; Acidovorax.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
"Complete sequence of chromosome 1 of Acidovorax sp. JS42.";
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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
CP000539; ABM43854.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_987930.1; -.
3D structure databases
ModBase A1WC79.
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 A1WC79.
Genome annotation databases
GeneID 4672286; -.
GenomeReviews CP000539_GR; Ajs_3745.
KEGG ajs:Ajs_3745; -.
CMR A1WC79; Ajs_3745.
Other
ProtoNet A1WC79.
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   347  347     Dihydroorotase. PRO_0000325566
METAL   17    17        Zinc 1 (By similarity). 
METAL   19    19        Zinc 1 (By similarity). 
METAL   102   102        Zinc 1; via carbamate group (By similarity). 
METAL   102   102        Zinc 2; via carbamate group (By similarity). 
METAL   139   139        Zinc 2 (By similarity). 
METAL   177   177        Zinc 2 (By similarity). 
METAL   250   250        Zinc 1 (By similarity). 
MOD_RES   102   102        N6-carboxylysine (By similarity). 
Sequence information
Length: 347 AA [This is the length of the unprocessed precursor] Molecular weight: 38041 Da [This is the MW of the unprocessed precursor] CRC64: 310D6DDF1B651282 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTATTDTLTI TRPDDWHLHV RDGEPLRTVV PHTAAQFGRA IIMPNLRPPV TTAQQAAEYK 

        70         80         90        100        110        120 
QRILAAVPEG VAFEPLMTLY LTDNLPPDEI ARARDAGVVA AKLYPAGATT NSDAGVTDLR 

       130        140        150        160        170        180 
KTYKTLEAMQ KAGLLLLVHG EVTSSDIDLF DREAVFIEQQ LIPLRRHFPE LKIVFEHITT 

       190        200        210        220        230        240 
KEAAQYVKEA GRFTAATITA HHLLYNRNAI FTGGIRPHYY CLPVLKREVH RQALVQAATS 

       250        260        270        280        290        300 
GSDKFFLGTD SAPHPAHLKE HATGCAGCYT AHAAIEMYAE AFDNAGALDK LEGFASVHGP 

       310        320        330        340 
AFYGLPRNTG TVTLRRESWT PPDSFAFGEA ALKPLRAGEA LPWRLVA
A1WC79 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!