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Reviewed, UniProtKB/Swiss-Prot Q81WF0 (PYRC_BACAN)

Last modified September 2, 2008. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

Names and origin

Protein namesRecommended name:
    Dihydroorotase
      Short name=DHOase
    EC=3.5.2.3
Gene names
Name: pyrC
Ordered Locus Names: BA_4027, GBAA4027, BAS3739
OrganismBacillus anthracis [Complete proteome] [HAMAP]
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H(2)O = N-carbamoyl-L-aspartate.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 3/6.

Subunit structure

Homodimer By similarity.

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: HAMAP

   Molecular functiondihydroorotase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Dihydroorotase
PRO_0000325582

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
Q81WF0-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 6AA9493906CCA956

FASTA42846,656
        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 RGKEDHEALI 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 

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed: 12721629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.
[3]"Bacillus anthracis comparative genomics."
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.

Cross-references

Sequence databases

AE016879 Genomic DNA. Translation: AAP27754.1.
AE017334 Genomic DNA. Translation: AAT33144.1.
AE017225 Genomic DNA. Translation: AAT56041.1.
RefSeqNP_846268.1.
YP_020669.1.
YP_029990.1.

3D structure databases

HSSPHSSP built from PDB template 1GKR based on UniProtKB P81006.
ModBaseSearch...

Protein family/group databases

MEROPSM38.972.

Genome annotation databases

GeneID1086660.
2819582.
2852141.
GenomeReviewsGene locus BA_4027 in contig AE016879_GR.
Gene locus BAS3739 in contig AE017225_GR.
Gene locus GBAA4027 in contig AE017334_GR.
KEGGban:BA4027.
bar:GBAA4027.
bat:BAS3739.
TIGRBA_4027.
GBAA4027.

Phylogenomic databases

HOGENOMQ81WF0.

Enzyme and pathway databases

BioCycBANT260799:BAS3739-MON.
BANT261594:GBAA4027-MON.

Family and domain databases

HAMAPMF_00220.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR004722. DHOmult.
IPR002195. Dihydroorotase_CS.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
ProDomPD000518. DHOase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00857. pyrC_multi. 1 hit.
PROSITEPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRC_BACAN
AccessionPrimary (citable) accession number: Q81WF0
Secondary accession number(s): Q6HUJ8, Q6KNT3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: June 1, 2003
Last modified: September 2, 2008
This is version 41 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)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

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