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 Q39US3


[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_GEOMG
Primary accession number Q39US3
Secondary accession numbers None
Integrated into Swiss-Prot on March 18, 2008
Sequence was last modified on March 18, 2008 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 23)
Name and origin of the protein
Protein name Dihydroorotase
Synonyms DHOase
EC 3.5.2.3
Gene name
Name: pyrC
OrderedLocusNames: Gmet_1770
From
Geobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210) [TaxID: 269799] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; Geobacteraceae; Geobacter.
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., Di Bartolo G., Chain P., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
"Complete sequence of Geobacter metallireducens GS-15.";
Submitted (OCT-2005) 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
CP000148; ABB32001.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_384726.1; -.
3D structure databases
ModBase Q39US3.
Enzyme and pathway databases
BioCyc GMET269799:GMET_1770-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 Q39US3.
Genome annotation databases
GeneID 3741446; -.
GenomeReviews CP000148_GR; Gmet_1770.
KEGG gme:Gmet_1770; -.
NMPDR fig|269799.3.peg.2087; -.
Phylogenomic databases
HOGENOM Q39US3; -.
Genome annotation databases
CMR Q39US3; Gmet_1770.
Other
ProtoNet Q39US3.
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   424  424     Dihydroorotase. PRO_0000325594
METAL   61    61        Zinc 1 (By similarity). 
METAL   63    63        Zinc 1 (By similarity). 
METAL   143   143        Zinc 1; via carbamate group (By similarity). 
METAL   143   143        Zinc 2; via carbamate group (By similarity). 
METAL   180   180        Zinc 2 (By similarity). 
METAL   233   233        Zinc 2 (By similarity). 
METAL   306   306        Zinc 1 (By similarity). 
MOD_RES   143   143        N6-carboxylysine (By similarity). 
Sequence information
Length: 424 AA [This is the length of the unprocessed precursor] Molecular weight: 44713 Da [This is the MW of the unprocessed precursor] CRC64: 0DC8AA0CE041462B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNLLIQGGRV IDPSQGIDEV LDILVENGAV KELGKGVKAP SGTETIDASG LIVTPGLIDM 

        70         80         90        100        110        120 
HVHLRDPGHE YKEDIVSGTK AAAAGGFTSV ACMPNTKPVN DNKAVTSYII AKAKAEGSVN 

       130        140        150        160        170        180 
VFPVGSITQG SKGELLSEMG ELKESGCVAV SDDGHPVTNS ELMRRALEYA KGMGIMVISH 

       190        200        210        220        230        240 
AEDLSLVGAG VMNEGFVSTE LGLKGIPWAA EDAATARDVY LAEFTDSPLH IAHVSTKGSL 

       250        260        270        280        290        300 
RIIRNAKARG VKVTCETAPH YFSLTDDAVR GYDTNAKMNP PLRTADDVTA VKEALKDGTI 

       310        320        330        340        350        360 
DAIATDHAPH HIDEKDLEFN EALNGIVGLE TSLTLSLRLV EEGVLTLPVL VDKMACNPAK 

       370        380        390        400        410        420 
ILGIDRGTLK PGSVADITVI DPKATWTVDA DKLASKSKNS PFLGWEVKGA AAFTIVGGKV 


VYKR 

Q39US3 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!