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Q97LN7 (PYRC_CLOAB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 74. 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:CA_C0519
OrganismClostridium acetobutylicum
Taxonomic identifier1488 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length424 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
Reference 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 – 424424Dihydroorotase HAMAP MF_00220_B
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

Sequences

Sequence LengthMass (Da)Tools
Q97LN7 [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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE001437 Genomic DNA. Translation: AAK78499.1.
PIRH96963.
RefSeqNP_347159.1. NC_003030.1.

3D structure databases

ProteinModelPortalQ97LN7.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1116702.
GenomeReviewsGene locus CA_C0519 in contig AE001437_GR.
KEGGcac:CA_C0519.
NMPDRfig|272562.1.peg.688.
PATRIC32035393. VBICloAce74127_0718.

Phylogenomic databases

HOGENOMHBG724623.
OMACDVHPVG.
PhylomeDBQ97LN7.
ProtClustDBPRK09357.

Enzyme and pathway databases

BioCycCACE272562:CAC0519-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. False negative.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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: January 25, 2012
This is version 74 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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