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UniProtKB/Swiss-Prot entry Q17W17


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

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Entry information
Entry name PYRC_HELAH
Primary accession number Q17W17
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on July 25, 2006 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 21)
Name and origin of the protein
Protein name Dihydroorotase
Synonyms DHOase
EC 3.5.2.3
Gene name
Name: pyrC
OrderedLocusNames: Hac_1431
From
Helicobacter acinonychis (strain Sheeba) [TaxID: 382638] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; Helicobacteraceae; Helicobacter.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1371/journal.pgen.0020120; PubMed=16789826 [NCBI, ExPASy, EBI, Israel, Japan]
Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G., Gressmann H., Achtman M., Schuster S.C.;
"Who ate whom? Adaptive Helicobacter genomic changes that accompanied a host jump from early humans to large felines.";
PLoS Genet. 2:1097-1110(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
AM260522; CAK00159.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_665158.1; -.
3D structure databases
ModBase Q17W17.
Enzyme and pathway databases
BioCyc HACI382638:HAC_1431-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 IPR004721; DHOdimr.
IPR002195; Dihydroorotase_CS.
Graphical view of domain structure.
PIRSF PIRSF001237; DHOdimr; 1.
TIGRFAMs TIGR00856; pyrC_dimer; 1.
PROSITE PS00482; DIHYDROOROTASE_1; 1.
PS00483; DIHYDROOROTASE_2; 1.
BLOCKS Q17W17.
Genome annotation databases
GeneID 4177751; -.
GenomeReviews AM260522_GR; Hac_1431.
KEGG hac:Hac_1431; -.
NMPDR fig|382638.8.peg.1385; -.
Phylogenomic databases
HOGENOM Q17W17; -.
Genome annotation databases
CMR Q17W17; Hac_1431.
Other
ProtoNet Q17W17.
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   339  339     Dihydroorotase. PRO_1000024016
METAL   12    12        Zinc 1 (By similarity). 
METAL   14    14        Zinc 1 (By similarity). 
METAL   94    94        Zinc 1; via carbamate group (By similarity). 
METAL   94    94        Zinc 2; via carbamate group (By similarity). 
METAL   133   133        Zinc 2 (By similarity). 
METAL   167   167        Zinc 2 (By similarity). 
METAL   239   239        Zinc 1 (By similarity). 
MOD_RES   94    94        N6-carboxylysine (By similarity). 
Sequence information
Length: 339 AA [This is the length of the unprocessed precursor] Molecular weight: 38001 Da [This is the MW of the unprocessed precursor] CRC64: F40860B3AF155A31 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEITLFDPID AHLHVREGVL LKAVLKYSSE PFSAAVIMPN LSKPLIDTQI TLEYEGEILK 

        70         80         90        100        110        120 
NSSNFKPLMS LYFNDGLTLE ELQHAKHQGI KFLKLYPKGM TTNAQNGTSD LLGEKTLEIL 

       130        140        150        160        170        180 
EDAQKLGFIL CIHAEQAGFC LDKEFLCHSV LETFAHSFPK LKIIIEHLSD WRSIALIEKH 

       190        200        210        220        230        240 
DNLYATLTLH HISMTLDDLL GGSLNPHCFC KPLIKTQKDQ ERLLSLALKA HPKISFGSDS 

       250        260        270        280        290        300 
APHVISKKHS ANIPAGIFSA PILLPALCEL FEKHNALENL QAFISDNAKK IYTLDNLPSK 

       310        320        330 
KVRLSKKPFI VPTHTLCLNE KIAILREGET LSWNIQEIA 

Q17W17 in FASTA format

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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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