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A3DE07 (PYRC_CLOTH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydroorotase
Short name=DHOase
EC=3.5.2.3
Gene names
Name:pyrC
Ordered Locus Names:Cthe_0952
OrganismClostridium thermocellum (strain ATCC 27405 / DSM 1237) [Complete proteome] [HAMAP]
Taxonomic identifier203119 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length426 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP MF_00220_B

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP MF_00220_B

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP MF_00220_B

Subunit structure

Homodimer By similarity. HAMAP MF_00220_B

Sequence similarities

Belongs to the DHOase family. Type 2 subfamily.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpyrimidine nucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functiondihydroorotase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 426426Dihydroorotase HAMAP MF_00220_B
PRO_0000325591

Sites

Metal binding581Zinc 1 By similarity
Metal binding601Zinc 1 By similarity
Metal binding1401Zinc 1; via carbamate group By similarity
Metal binding1401Zinc 2; via carbamate group By similarity
Metal binding1771Zinc 2 By similarity
Metal binding2301Zinc 2 By similarity
Metal binding3031Zinc 1 By similarity

Amino acid modifications

Modified residue1401N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A3DE07 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: 9125BD0F8FFA02A4

FASTA42646,253
        10         20         30         40         50         60 
MLIKGGHVVD PKTNTNGIMD ILVEDGIITE IGKDIEISNG DIIYAEGKLV LPGLVDAHCH 

        70         80         90        100        110        120 
LRDPGFEYKE DIETGTMSAA MGGFTSIACM PNTDPVCDNK AVVKYIINKA KQDGYVNVYP 

       130        140        150        160        170        180 
IGAISKGQKG EELSEIGELK FAGAVAISDD GKPVKSSSLM KRALEYSSMF DIAVISHCED 

       190        200        210        220        230        240 
LDLADGGVMN EGYWSTVMGL KGIPSAAEEI MVARDIILSE YTKVPIHIAH VSTELSVELI 

       250        260        270        280        290        300 
RNAKKRGVKV TCETCPHYFV LTDEACKDFN TLAKVNPPLR TRRDVEAVIE GLKDGTIDII 

       310        320        330        340        350        360 
ATDHAPHHAD EKNVEFNLAA NGMVGFETAL PLAITYLVKP GHLTISQLVE KMCVNPSKLL 

       370        380        390        400        410        420 
GINKGTLETG RSADITIVDL NEEFVVDVNK FKSKSKNSPF HGFKLNGSVY YTLVNGNVVV 


REKVLL

« Hide

References

[1]"Complete sequence of Clostridium thermocellum ATCC 27405."
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., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D., Newcomb M., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27405 / DSM 1237.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000568 Genomic DNA. Translation: ABN52186.1.
RefSeqYP_001037379.1. NC_009012.1.

3D structure databases

ProteinModelPortalA3DE07.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3DE07.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4811245.
GenomeReviewsGene locus Cthe_0952 in contig CP000568_GR.
KEGGcth:Cthe_0952.
NMPDRfig|203119.1.peg.435.
PATRIC19515625. VBICloThe47081_0999.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0044.
HOGENOMHBG724623.
OMACDVHPVG.
ProtClustDBCLSK2471753.

Family and domain databases

HAMAPMF_00220_B. PyrC_type2_B.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR004722. DHOase.
IPR002195. Dihydroorotase_CS.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
KOK01465.
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMSSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMsTIGR00857. PyrC_multi. 1 hit.
PROSITEPS00482. DIHYDROOROTASE_1. False negative.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRC_CLOTH
AccessionPrimary (citable) accession number: A3DE07
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 20, 2007
Last modified: December 14, 2011
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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