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B2TNG1 (PYRC_CLOBB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 26. 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:CLL_A2579
OrganismClostridium botulinum (strain Eklund 17B / Type B) [Complete proteome] [HAMAP]
Taxonomic identifier508765 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length398 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 – 398398Dihydroorotase HAMAP MF_00220_B
PRO_1000100073

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 binding1781Zinc 2 By similarity
Metal binding2151Zinc 2 By similarity
Metal binding2831Zinc 1 By similarity

Amino acid modifications

Modified residue1401N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B2TNG1 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: E984AEADD0456300

FASTA39844,230
        10         20         30         40         50         60 
MELLIKNARI IDAIQDFKGD IYIKDGVINE IAQEIKKDNV EVLNCEEKIL MPAFIDTHAH 

        70         80         90        100        110        120 
FRDPGLTCKE DLESGSKAAL RGGYTGVCLM ANTKPICSSK EVVQYVRDKS KELDLIDIHQ 

       130        140        150        160        170        180 
CISVTQNFDG KTLDHLNEFK DDNEVKAISD DGVGVSNSNI MLEAMKIAKE NNWVLMSHAE 

       190        200        210        220        230        240 
SPEFSKSDMR IAENMMTIRD VELAKLSGAH VHMCHVSTKE ALKCIIAAKD EGANITLEVT 

       250        260        270        280        290        300 
PHHIGLTKEI NDYRVNPPIR EKEDVEEIIK AIKMGNVDTI GTDHAPHTLE EKSKGSPGMV 

       310        320        330        340        350        360 
GLETAFPICY TKLVRENGVS LNELSKLMSL NPARLLGMNK GRISIGVEAD LVLIDIDKKI 

       370        380        390 
KVDSNEFVSK GRNTPFEGME YYGEVLATIK SGKIKYKK

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References

[1]"Complete sequence of Clostridium botulinum strain Eklund."
Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., Sutton G., Brettin T.S.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Eklund 17B / Type B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001056 Genomic DNA. Translation: ACD22973.1.
RefSeqYP_001886768.1. NC_010674.1.

3D structure databases

ProteinModelPortalB2TNG1.
ModBaseSearch...

Protein-protein interaction databases

STRINGB2TNG1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6294728.
GenomeReviewsGene locus CLL_A2579 in contig CP001056_GR.
KEGGcbk:CLL_A2579.
PATRIC19397976. VBICloBot123574_2493.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG724623.
OMASHAESPE.
ProtClustDBCLSK899305.

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_CLOBB
AccessionPrimary (citable) accession number: B2TNG1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: January 25, 2012
This is version 26 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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