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UniProtKB/Swiss-Prot entry A4J556

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

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Entry information
Entry name PYRC_DESRM
Primary accession number A4J556
Secondary accession numbers None
Integrated into Swiss-Prot on February 26, 2008
Sequence was last modified on May 1, 2007 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 12)
Name and origin of the protein
Protein name Dihydroorotase
Synonyms DHOase
EC 3.5.2.3
Gene name
Name: pyrC
OrderedLocusNames: Dred_1682
From
Desulfotomaculum reducens (strain MI-1) [TaxID: 349161] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae; Desulfotomaculum.
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 del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
"Complete sequence of Desulfotomaculum reducens MI-1.";
Submitted (MAR-2007) 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
CP000612; ABO50209.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001113034.1; -.
3D structure databases
ModBase A4J556.
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 A4J556.
Genome annotation databases
GeneID 4957126; -.
GenomeReviews CP000612_GR; Dred_1682.
KEGG drm:Dred_1682; -.
CMR A4J556; Dred_1682.
Other
ProtoNet A4J556.
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_1000071754
METAL   59    59        Zinc 1 (By similarity). 
METAL   61    61        Zinc 1 (By similarity). 
METAL   140   140        Zinc 1; via carbamate group (By similarity). 
METAL   140   140        Zinc 2; via carbamate group (By similarity). 
METAL   177   177        Zinc 2 (By similarity). 
METAL   230   230        Zinc 2 (By similarity). 
METAL   303   303        Zinc 1 (By similarity). 
MOD_RES   140   140        N6-carboxylysine (By similarity). 
Sequence information
Length: 427 AA [This is the length of the unprocessed precursor] Molecular weight: 45864 Da [This is the MW of the unprocessed precursor] CRC64: D9A87C2646FBB20C [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MRYLIKGGIV VDPVADTLTC TDILVEEGMI KEIGQLSDSE AEVIAAEGNY VCPGFMDMHV 

        70         80         90        100        110        120 
HLREPGYEYK EDIVSGTRAA AMGGFTSVAC MPNTNPVADN AAIISHVLAK ARNAAARVFP 

       130        140        150        160        170        180 
IGALTKGSLG KELTEMADLK GAGAVALSDD GMPVMNADIM LRVMQYASML EMTVISHCED 

       190        200        210        220        230        240 
NKLSEGGQMH EGAVSAMLGL KGIPSLAEEI MVARDILLSE YTGCRLHLAH ISTEGSVRLV 

       250        260        270        280        290        300 
RQAKERGVPV TAEATPHHFT LTEEAVQGYS TNAKVNPPLR RQTDVEAIKE GLRDGTIDVI 

       310        320        330        340        350        360 
ATDHAPHAYH EKDVEFQYAP NGMIGLETAV GLIFTQLVQP GILTVPQAVA KLTCNPHRVL 

       370        380        390        400        410        420 
GLSGGRLLPG TPANITIIDP KLSEVVDPTK LLSKSKNTPF GRWKLTGLPV LTMKDGLLVM 


RDRQLLE
A4J556 in FASTA format

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