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 Q2IIB0

[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_ANADE
Primary accession number Q2IIB0
Secondary accession numbers None
Integrated into Swiss-Prot on March 18, 2008
Sequence was last modified on March 7, 2006 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 22)
Name and origin of the protein
Protein name Dihydroorotase
Synonyms DHOase
EC 3.5.2.3
Gene name
Name: pyrC
OrderedLocusNames: Adeh_1619
From
Anaeromyxobacter dehalogenans (strain 2CP-C) [TaxID: 290397] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; Cystobacterineae; Myxococcaceae; Anaeromyxobacter.
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 T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
Submitted (JAN-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
CP000251; ABC81392.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_464829.1; -.
3D structure databases
ModBase Q2IIB0.
Enzyme and pathway databases
BioCyc ADEH290397:ADEH_1619-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.
TIGRFAMs TIGR00857; pyrC_multi; 1.
PROSITE PS00482; DIHYDROOROTASE_1; 1.
PS00483; DIHYDROOROTASE_2; 1.
BLOCKS Q2IIB0.
Genome annotation databases
GeneID 3888118; -.
GenomeReviews CP000251_GR; Adeh_1619.
KEGG ade:Adeh_1619; -.
Phylogenomic databases
HOGENOM Q2IIB0; -.
Genome annotation databases
CMR Q2IIB0; Adeh_1619.
Other
ProtoNet Q2IIB0.
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   433  433     Dihydroorotase. PRO_0000325580
METAL   63    63        Zinc 1 (By similarity). 
METAL   65    65        Zinc 1 (By similarity). 
METAL   145   145        Zinc 1; via carbamate group (By similarity). 
METAL   145   145        Zinc 2; via carbamate group (By similarity). 
METAL   182   182        Zinc 2 (By similarity). 
METAL   235   235        Zinc 2 (By similarity). 
METAL   310   310        Zinc 1 (By similarity). 
MOD_RES   145   145        N6-carboxylysine (By similarity). 
Sequence information
Length: 433 AA [This is the length of the unprocessed precursor] Molecular weight: 45437 Da [This is the MW of the unprocessed precursor] CRC64: 36351670669BD114 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSDVLFIEGG RVIDPAGGVD GVRTVVIRDG KVAEVAERVE RPRDARVLDA RNRWVTPGFV 

        70         80         90        100        110        120 
DLHVHLREPG QEYKETVATG ARAAVAGGFT AVCAMPNTKP VNDCAAVTEL VLARAAAAGL 

       130        140        150        160        170        180 
ARVYPVGAIS KGSGGEELAE YGELKASGCV ALSDDGRPVM SSALMRRALE YARAFGLPLT 

       190        200        210        220        230        240 
VHEEDLHLVG KGVMHEGAAA TRLGLKGIPS QAEDVMVLRD IALVELTGGR LHVAHVSTAG 

       250        260        270        280        290        300 
AVRAIREAKR RGLPVTGEVT PHHLALTDDD VAASGYSTDF KMNPPLRSAD DVRACREGLA 

       310        320        330        340        350        360 
DGTLDAIATD HAPHSAVEKD VEFDAAANGI VGLETAFSVC LGLVREGALT ERRLVEALTA 

       370        380        390        400        410        420 
GPARVFGLPA GTLARGAAAD VAVLDAAAEW TLDPARLQSK GRNTPWKGRR LAGRCTHTIV 

       430 
GGRIVHEEGK ADR
Q2IIB0 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 ca flag CBR Canada Mirror sites: Australia Brazil China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!