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P25995 (PYRC_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydroorotase
Short name=DHOase
EC=3.5.2.3
Gene names
Name:pyrC
Ordered Locus Names:BSU15500
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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.

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 – 428428Dihydroorotase HAMAP MF_00220_B
PRO_0000147229

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

Experimental info

Sequence conflict811A → G in AAA21268. Ref.1
Sequence conflict220 – 2223AEA → LG in AAA21268. Ref.1
Sequence conflict323 – 35129GIVGL…KQLID → RNCRLRNSIPASLHTLCQKW QLVTEAADLT in AAA21268. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P25995 [UniParc].

Last modified June 16, 2009. Version 2.
Checksum: 86739BFB81D395AB

FASTA42846,533
        10         20         30         40         50         60 
MSYLIKNGWI LNENGEKTQA DIRVTGETIT AIGKLDATDN ETVIDAKGLL VSPGFVDLHV 

        70         80         90        100        110        120 
HFREPGGEKK ETIETGAKAA ARGGYTTVAA MPNTRPVPDT KEQMEWVQNR IKETSCVRVL 

       130        140        150        160        170        180 
PYASITIRQI GDEMTNFEAL KEAGAFAFTD DGVGIQTAGM MYEAMKRAAA IDKAIVAHCE 

       190        200        210        220        230        240 
DNSLIYGGSV HEGTFSKANG LNGIPSVCES VHIARDVLLA EAANCHYHVC HISTKESVRV 

       250        260        270        280        290        300 
VRDAKKAGIR VTAEVSPHHL LLCDEDIPGL DTNYKMNPPL RSPEDRAALI EGLLDGTIDF 

       310        320        330        340        350        360 
IATDHAPHTE EEKNTEMKLA PFGIVGLETA FPLLYTHFVK NGSWSLKQLI DYMTIKPCEA 

       370        380        390        400        410        420 
FGLPYGTLQT GQAADITLID LEKEAVIDKE TFLSKGKNTP FNGISCTGWP VATIAAGKLA 


YEEGRLVK

« Hide

References

« Hide 'large scale' references
[1]"Functional organization and nucleotide sequence of the Bacillus subtilis pyrimidine biosynthetic operon."
Quinn C.L., Stephenson B.T., Switzer R.L.
J. Biol. Chem. 266:9113-9127(1991) [PubMed: 1709162] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract]
Cited for: SEQUENCE REVISION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M59757 Genomic DNA. Translation: AAA21268.1.
AL009126 Genomic DNA. Translation: CAB13424.2.
PIRDEBSO. D39845.
RefSeqNP_389433.2. NC_000964.3.

3D structure databases

ProteinModelPortalP25995.
SMRP25995. Positions 4-422.
ModBaseSearch...

Protein family/group databases

MEROPSM38.972.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000000984; EBBACP00000000984; EBBACG00000000982.
GeneID937095.
GenomeReviewsGene locus BSU15500 in contig AL009126_GR.
KEGGbsu:BSU15500.
NMPDRfig|224308.1.peg.1552.
PATRIC18974907. VBIBacSub10457_1645.

Organism-specific databases

GenoListBSU15500. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000001626.
HOGENOMHBG724623.
PhylomeDBP25995.
ProtClustDBCLSK887279.

Enzyme and pathway databases

BioCycBSUB:BSU15500-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_BACSU
AccessionPrimary (citable) accession number: P25995
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: June 16, 2009
Last modified: January 25, 2012
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents