Skip Header

Contribute Send feedback
Read comments (?) or add your own

B0JQJ1 (PYRC_MICAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:MAE_08280
OrganismMicrocystis aeruginosa (strain NIES-843) [Complete proteome] [HAMAP]
Taxonomic identifier449447 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Chroococcales › Microcystis

Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP MF_00219

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP MF_00219

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP MF_00219

Subunit structure

Homodimer By similarity. HAMAP MF_00219

Sequence similarities

Belongs to the DHOase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpyrimidine base biosynthetic process

Inferred from electronic annotation. Source: InterPro

pyrimidine 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 – 344344Dihydroorotase HAMAP MF_00219
PRO_1000078098

Sites

Metal binding131Zinc 1 By similarity
Metal binding151Zinc 1 By similarity
Metal binding991Zinc 1; via carbamate group By similarity
Metal binding991Zinc 2; via carbamate group By similarity
Metal binding1361Zinc 2 By similarity
Metal binding1741Zinc 2 By similarity
Metal binding2471Zinc 1 By similarity

Amino acid modifications

Modified residue991N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B0JQJ1 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: ADC2443A9A9E8C13

FASTA34438,398
        10         20         30         40         50         60 
MRRLTMTRPD DWHLHLRDGA AMKAVLPHTV RQFARAIIMP NLKPPVRSVA DAASYRERIL 

        70         80         90        100        110        120 
AAVPEGQQFE PLMTLYLTDN TSPEEIVAAK ASQFVKAVKY YPAGATTNSD LGVTDLRRCD 

       130        140        150        160        170        180 
GVLAAMEQVD MPLLLHGEVT DGDIDVFDRE KVFIEKHLIP LITRFPKLRV VFEHITTADA 

       190        200        210        220        230        240 
VKFVLSANNN VAATITPQHL LFSRNILFTG GIRPHFYCLP ILKREDHRLA LLQAATSGNP 

       250        260        270        280        290        300 
KFFLGTDSAP HSRYSKESSC GCAGCYSALH ALELYAEAFE SVDAIDQLEG FASFHGPDFY 

       310        320        330        340 
QLPRNTEQIT LTKSPWRIPD ELPFPESGLV PLRAGEEITW QLGE

« Hide

References

[1]"Complete genomic structure of the bloom-forming toxic cyanobacterium Microcystis aeruginosa NIES-843."
Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M., Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A., Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M. expand/collapse author list , Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.
DNA Res. 14:247-256(2007) [PubMed: 18192279] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NIES-843.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP009552 Genomic DNA. Translation: BAG00650.1.
RefSeqYP_001655842.1. NC_010296.1.

3D structure databases

ProteinModelPortalB0JQJ1.
SMRB0JQJ1. Positions 3-342.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0JQJ1.

Proteomic databases

PRIDEB0JQJ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5861626.
GenomeReviewsGene locus MAE_08280 in contig AP009552_GR.
KEGGmar:MAE_08280.
PATRIC22626859. VBIMicAer59304_0769.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628648.
OMACLPVAKR.
PhylomeDBB0JQJ1.
ProtClustDBPRK05451.

Enzyme and pathway databases

BioCycMAER449447:MAE_08280-MONOMER.

Family and domain databases

HAMAPMF_00219. PyrC_type1.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR004721. DHOdimr.
IPR002195. Dihydroorotase_CS.
[Graphical view]
KOK01465.
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
PIRSFPIRSF001237. DHOdimr. 1 hit.
TIGRFAMsTIGR00856. PyrC_dimer. 1 hit.
PROSITEPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRC_MICAN
AccessionPrimary (citable) accession number: B0JQJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 18, 2008
Last modified: January 25, 2012
This is version 28 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

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