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 P57416


[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_BUCAI
Primary accession number P57416
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 2000
Sequence was last modified on December 1, 2000 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 50)
Name and origin of the protein
Protein name Dihydroorotase
Synonyms DHOase
EC 3.5.2.3
Gene name
Name: pyrC
OrderedLocusNames: BU334
From
Buchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum symbiotic bacterium) [TaxID: 118099] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tokyo 1998;
DOI=10.1038/35024074; PubMed=10993077 [NCBI, ExPASy, EBI, Israel, Japan]
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS.";
Nature 407:81-86(2000).
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
BA000003; BAB13039.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_240153.1; -.
3D structure databases
HSSP P05020; 1J79. [HSSP ENTRY / PDB]
ModBase P57416.
Enzyme and pathway databases
BioCyc BSP107806:BU334-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 P57416.
Genome annotation databases
GeneID 1110030; -.
GenomeReviews BA000003_GR; BU334.
KEGG buc:BU334; -.
Phylogenomic databases
HOGENOM P57416; -.
Genome annotation databases
CMR P57416; BU334.
Other
ProtoNet P57416.
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   350  350     Dihydroorotase. PRO_0000147203
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: 350 AA [This is the length of the unprocessed precursor] Molecular weight: 40416 Da [This is the MW of the unprocessed precursor] CRC64: 41D16017597B52DC [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSKFVKKIKI IKPDDWHVHL RDNEILNQVI KYTGKFYKRA VIMPNLNSPI TSCLKSIAYR 

        70         80         90        100        110        120 
NRILKSMHLN YKFKPLMTCY LTNSTSPKEL EFGFSKKIFV AAKFYPNGCT TNSKTGIKKI 

       130        140        150        160        170        180 
SDITPVLECM EKIGMPLLIH GEEINQNIDI YDREAKFIEK TLDPLRKKFP KLKIVLEHIT 

       190        200        210        220        230        240 
TKESVEYIKN NDVNYLSATI TPHHLMLNRN DMFYGGIQPY LYCLPILKKN KHRMALRKAI 

       250        260        270        280        290        300 
SNGDKHFFLG SDTAPHLHKN KINMLGCAGI FNAPSSLLSY VKVFEEMRAL KYLQSFCSEN 

       310        320        330        340        350 
GPKFYNMPIN KETITIIKKP CKIIKKINVG RNVIIPFLSG EILNWSIESD 

P57416 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!