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Reviewed, UniProtKB/Swiss-Prot Q97LN7 (PYRC_CLOAB)

Last modified February 9, 2010. Version 63. 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: CA_C0519
OrganismClostridium acetobutylicum [Complete proteome] [HAMAP]
Taxonomic identifier1488 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

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Protein attributes

Sequence length424 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 – 424424Dihydroorotase HAMAP MF_00220
PRO_0000147231

Sites

Metal binding601Zinc 1 By similarity
Metal binding621Zinc 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
Q97LN7-1 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 4A8D60A4726F473D

FASTA42446,528
        10         20         30         40         50         60 
MIIIKNGYVI DPLTKREGKF DILIDGENVV RISQDIGIDD DIEVIDAEDC IVSPGFIDIH 

        70         80         90        100        110        120 
SHFRDPGFTE KEDIITGARA AARGGYTTVI CMANTNPVVD NVETLRYIVD KAKTAKIEVL 

       130        140        150        160        170        180 
QVGTITKGMQ GVELVDMEAL KEAGAVGFSD DGKPIMDSRL VLEAMQKARE LDVPLSFHEE 

       190        200        210        220        230        240 
DPKLVYESGI NGGKVAEKLN MMGALEEAET VLTARDAALA VSSGAKTNIQ HISSKISLGI 

       250        260        270        280        290        300 
IKLAKEMGAN IIAEATPQHF SITEEEILNC GTNAKVNPPL RREDDRKAIV AALKDDTIQV 

       310        320        330        340        350        360 
IATDHAPHTK DEKAREFKEA PSGMIGLETA LSLAVTNLVK TGDLTYRDMI SKLTINPARF 

       370        380        390        400        410        420 
YNLDRGYIKE GHRADIVIFD PDEKYTVKEE EFQSKASNSP FIGKELFGKV KTTIYNGKIV 


YEDK

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References

[1]"Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum."
Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.
J. Bacteriol. 183:4823-4838(2001) [PubMed: 11466286] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE001437 Genomic DNA. Translation: AAK78499.1.
PIRH96963.
RefSeqNP_347159.1.

3D structure databases

SMRQ97LN7. Positions 1-423.
ModBaseSearch...

Genome annotation databases

GeneID1116702.
GenomeReviewsGene locus CA_C0519 in contig AE001437_GR.
KEGGcac:CAC0519.
NMPDRfig|272562.1.peg.688.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG724623.
OMAVTTVVCQ.
PhylomeDBQ97LN7.

Enzyme and pathway databases

BioCycCACE272562:CAC0519-MONOMER.
BRENDA3.5.2.3. 2866.

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

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Entry information

Entry namePYRC_CLOAB
AccessionPrimary (citable) accession number: Q97LN7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: October 1, 2001
Last modified: February 9, 2010
This is version 63 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