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Q636D8 (PYRC_BACCZ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. 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:BCE33L3647
OrganismBacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP]
Taxonomic identifier288681 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length428 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 – 428428Dihydroorotase HAMAP MF_00220_B
PRO_0000325585

Sites

Metal binding591Zinc 1 By similarity
Metal binding611Zinc 1 By similarity
Metal binding1411Zinc 1; via carbamate group By similarity
Metal binding1411Zinc 2; via carbamate group By similarity
Metal binding1781Zinc 2 By similarity
Metal binding2311Zinc 2 By similarity
Metal binding3041Zinc 1 By similarity

Amino acid modifications

Modified residue1411N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q636D8 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 7769493E6B0ED093

FASTA42846,598
        10         20         30         40         50         60 
MNYLFKNGRY MNEEGKIVAT DLLVQDGKIA KVAENITADN AEVIDVNGKL IAPGLVDVHV 

        70         80         90        100        110        120 
HLREPGGEHK ETIETGTLAA AKGGFTTICA MPNTRPVPDC REHMEDLQNR IKEKAHVNVL 

       130        140        150        160        170        180 
PYGAITVRQA GSEMTDFETL KELGAFAFTD DGVGVQDASM MLAAMKRAAK LNMAVVAHCE 

       190        200        210        220        230        240 
ENTLINKGCV HEGKFSEKHG LNGIPSVCES VHIARDILLA EAADCHYHVC HVSTKGSVRV 

       250        260        270        280        290        300 
IRDAKRAGIK VTAEVTPHHL VLCEDDIPSA DPNFKMNPPL RGKEDHAALI EGLLDGTIDM 

       310        320        330        340        350        360 
IATDHAPHTA EEKAQGIERA PFGITGFETA FPLLYTNLVK KGIITLEQLI QFLTEKPADT 

       370        380        390        400        410        420 
FGLEAGRLKE GRTADITIID LEQEEEIDPT TFLSKGKNTP FAGWKCQGWP VMTIVGGKIA 


WQKESALV 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000001 Genomic DNA. Translation: AAU16619.1.
RefSeqYP_085229.1. NC_006274.1.

3D structure databases

HSSPHSSP built from PDB template 1XRT based on UniProtKB O66990.
ProteinModelPortalQ636D8.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ636D8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000045051; EBBACP00000043952; EBBACG00000045042.
GeneID3024601.
GenomeReviewsGene locus BCE33L3647 in contig CP000001_GR.
KEGGbcz:BCZK3647.
PATRIC18891046. VBIBacCer95304_3861.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0044.
GeneTreeEBGT00050000001626.
HOGENOMHBG724623.
OMACDVHPVG.
PhylomeDBQ636D8.
ProtClustDBPRK09357.

Enzyme and pathway databases

BioCycBCER288681:BCE33L3647-MONOMER.

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. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRC_BACCZ
AccessionPrimary (citable) accession number: Q636D8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 49 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