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Reviewed, UniProtKB/Swiss-Prot Q9K9V7 (PYRC_BACHD)

Last modified February 9, 2010. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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 [Complete proteome] [HAMAP]
Taxonomic identifier86665 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP MF_00220

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP MF_00220

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP MF_00220

Subunit structure

Homodimer By similarity. HAMAP MF_00220

Sequence similarities

Belongs to the DHOase family. Type 2 subfamily.

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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: HAMAP

   Molecular functiondihydroorotase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Dihydroorotase HAMAP MF_00220
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

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Sequences

Sequence LengthMass (Da)Tools
Q9K9V7-1 [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

« Hide

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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 / C-125 / DSM 18197 / FERM 7344 / JCM 9153.

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Cross-references

Sequence databases

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

3D structure databases

SMRQ9K9V7. Positions 3-424.
ModBaseSearch...

Protein family/group databases

MEROPSM38.972.

Genome annotation databases

GeneID891500.
GenomeReviewsGene locus BH2538 in contig BA000004_GR.
KEGGbha:BH2538.
NMPDRfig|272558.1.peg.2538.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG724623.
OMAVTTVVCQ.
PhylomeDBQ9K9V7.

Enzyme and pathway databases

BioCycBHAL272558:BH2538-MONOMER.
BRENDA3.5.2.3. 191865.

Family and domain databases

HAMAPMF_00220_B. PyrC_type2_B.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR004722. DHOmult.
IPR002195. Dihydroorotase_CS.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR00857. pyrC_multi. 1 hit.
PROSITEPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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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: February 9, 2010
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents