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Q9K9V7 (PYRC_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 82. 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:BH2538
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

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_0000147228

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
Q9K9V7 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 657F6B920F62B32E

FASTA42846,284
        10         20         30         40         50         60 
MKTLIKNGSI VTKEGTVKTQ DVLLHDGVIS AIGLNLEETD AHVIEANGKL VTPGLVDLHV 

        70         80         90        100        110        120 
HLREPGGEAK ETIETGTKAA AKGGFTTVAA MPNTRPVPDS AEQMSWLTGR IDETGVVRVL 

       130        140        150        160        170        180 
PYAAITTRQL GRELTDFAKL KEAGAFAFTD DGVGVQSAAM MLEAMKEAAK LEMAIVAHCE 

       190        200        210        220        230        240 
ENTLIQNGSV HEGVFSKKHG IAGIPSVCES VHIARDVLLA EAAGVHYHVC HISTKESVRV 

       250        260        270        280        290        300 
VRDAKRAGIR VTAEVTPHHL LLCDEDIPGL DAHYKMNPPL RGKEDREALI EGLLDGTIDF 

       310        320        330        340        350        360 
IATDHAPHTE EEKGQGMERA PFGIVGLETA FPLLYTHFVK KGTFTLKQLV DWLTIDPAET 

       370        380        390        400        410        420 
FQLPYGRLEE GAPADVTIID LEAERAIDPA HFASKGRNTP FAGWTCQGWP VATLVGGKLV 


WEEKEVAR 

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References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000004 Genomic DNA. Translation: BAB06257.1.
PIRB83967.
RefSeqNP_243404.1. NC_002570.2.

3D structure databases

ProteinModelPortalQ9K9V7.
ModBaseSearch...

Protein family/group databases

MEROPSM38.972.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000053628; EBBACP00000052267; EBBACG00000053619.
GeneID891500.
GenomeReviewsGene locus BH2538 in contig BA000004_GR.
KEGGbha:BH2538.
NMPDRfig|272558.1.peg.2538.
PATRIC18942268. VBIBacHal18977_2647.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000001626.
HOGENOMHBG724623.
OMACDVHPVG.
PhylomeDBQ9K9V7.
ProtClustDBPRK09357.

Enzyme and pathway databases

BioCycBHAL272558:BH2538-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_BACHD
AccessionPrimary (citable) accession number: Q9K9V7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 82 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