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 Q5WFJ0

[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_BACSK
Primary accession number Q5WFJ0
Secondary accession numbers None
Integrated into Swiss-Prot on March 18, 2008
Sequence was last modified on November 23, 2004 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 25)
Name and origin of the protein
Protein name Dihydroorotase
Synonyms DHOase
EC 3.5.2.3
Gene name
Name: pyrC
OrderedLocusNames: ABC2335
From
Bacillus clausii (strain KSM-K16) [TaxID: 66692] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.;
"The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16.";
Submitted (OCT-2003) 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
AP006627; BAD64870.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_175831.1; -.
3D structure databases
ModBase Q5WFJ0.
Enzyme and pathway databases
BioCyc BCLA66692:ABC2335-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; 1.
PS00483; DIHYDROOROTASE_2; 1.
BLOCKS Q5WFJ0.
Genome annotation databases
GeneID 3202825; -.
GenomeReviews AP006627_GR; ABC2335.
KEGG bcl:ABC2335; -.
NMPDR fig|66692.3.peg.2023; -.
Phylogenomic databases
HOGENOM Q5WFJ0; -.
Genome annotation databases
CMR Q5WFJ0; ABC2335.
Other
ProtoNet Q5WFJ0.
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   427  427     Dihydroorotase. PRO_0000325587
METAL   57    57        Zinc 1 (By similarity). 
METAL   59    59        Zinc 1 (By similarity). 
METAL   139   139        Zinc 1; via carbamate group (By similarity). 
METAL   139   139        Zinc 2; via carbamate group (By similarity). 
METAL   176   176        Zinc 2 (By similarity). 
METAL   229   229        Zinc 2 (By similarity). 
METAL   302   302        Zinc 1 (By similarity). 
MOD_RES   139   139        N6-carboxylysine (By similarity). 
Sequence information
Length: 427 AA [This is the length of the unprocessed precursor] Molecular weight: 45862 Da [This is the MW of the unprocessed precursor] CRC64: C207AABD1D32A4CC [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAMKVTGGFI LDENGEQVAK DVYIKDGKIV EHVADGDIRQ QFDATGLLIS PGFVDVHVHL 

        70         80         90        100        110        120 
REPGGEKKET IETGTKAAAR GGFTTVAAMP NTRPVPDNAE QLDLLQARIS ETAVVRVLPY 

       130        140        150        160        170        180 
ASITTRQLGQ ELTDFKALKE AGAFAFTDDG VGIQEAGMML SAMKEAAALN MAVVAHCEDN 

       190        200        210        220        230        240 
SLINGGAVHE GHYAKAHGLN GIPSVCEAVH IARDVLLAEA AGAHYHVCHV STKESVRTIR 

       250        260        270        280        290        300 
DAKKAGIRVT AEVTPHHLLL CEDDIIGKDP NFKMNPPLRA KEDRDALVAG LLDGTIDFIA 

       310        320        330        340        350        360 
TDHAPHTAEE KSASLERAPF GIVGLETAFP LLYTHFVKPG TFTLKQLIDW LTVKPAQTFN 

       370        380        390        400        410        420 
LPYGTLQVGA AADLTLIDLK ANETIDPSMF LSKGKNTPFA GWDCAGIPQA TMVAGKTVYK 


KERITNE
Q5WFJ0 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!