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Q3AYG9 (PYRC_SYNS9) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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

Names and origin

Protein namesRecommended name:
Dihydroorotase

Short name=DHOase
EC=3.5.2.3
Gene names
Name:pyrC
Ordered Locus Names:Syncc9902_0892
OrganismSynechococcus sp. (strain CC9902) [Complete proteome] [HAMAP]
Taxonomic identifier316279 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length343 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP-Rule MF_00219

Pathway

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

Subunit structure

Homodimer By similarity. HAMAP-Rule 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_process'de novo' UMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

pyrimidine nucleobase biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functiondihydroorotase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 343343Dihydroorotase HAMAP-Rule MF_00219
PRO_1000024069

Sites

Metal binding141Zinc 1 By similarity
Metal binding161Zinc 1 By similarity
Metal binding1001Zinc 1; via carbamate group By similarity
Metal binding1001Zinc 2; via carbamate group By similarity
Metal binding1371Zinc 2 By similarity
Metal binding1751Zinc 2 By similarity
Metal binding2481Zinc 1 By similarity

Amino acid modifications

Modified residue1001N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3AYG9 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 8479D756696FD2CE

FASTA34338,057
        10         20         30         40         50         60 
MSDQIQLIAP DDWHVHLRDG EMLKQVVPYT AQMFRRAIVM PNLRPPVVTV EAAKAYRDQI 

        70         80         90        100        110        120 
VAACHPNWGF TPLMTAYLTD DIAPEEIERG FHEGVFTAAK LYPANATTNS AAGVTELRHI 

       130        140        150        160        170        180 
HGVLLVMERI GMPLLIHGEV TDVDVDVFDR EAVFIERSLK PIRDRYPGLK VVLEHITTEQ 

       190        200        210        220        230        240 
AVDFVGSADQ NLAATITPHH LHINRNAMFA GGLRSDFYCL PVAKRERHRL ALRRAAMSGD 

       250        260        270        280        290        300 
RRFFLGTDSA PHARPGKESS CGCAGIFNAP HALESYAMAF AQDDKLDKLE AFASLHGPAF 

       310        320        330        340 
YGLPVNEGIV TLQRDDKLVP NVVNGLVPFH AGETLPWRLQ PCT 

« Hide

References

[1]"Complete sequence of Synechococcus sp. CC9902."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CC9902.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000097 Genomic DNA. Translation: ABB25858.1.
RefSeqYP_376902.1. NC_007513.1.

3D structure databases

ProteinModelPortalQ3AYG9.
SMRQ3AYG9. Positions 2-340.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316279.Syncc9902_0892.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB25858; ABB25858; Syncc9902_0892.
GeneID3743497.
KEGGsye:Syncc9902_0892.
PATRIC23799033. VBISynSp76179_0979.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0418.
HOGENOMHOG000256259.
KOK01465.
OMAYAEAFEQ.
OrthoDBEOG6TFCMH.
ProtClustDBPRK05451.

Enzyme and pathway databases

BioCycSSP316279:GJCI-903-MONOMER.
UniPathwayUPA00070; UER00117.

Family and domain databases

HAMAPMF_00219. PyrC_type1.
InterProIPR006680. Amidohydro_1.
IPR004721. DHOdimr.
IPR002195. Dihydroorotase_CS.
[Graphical view]
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_SYNS9
AccessionPrimary (citable) accession number: Q3AYG9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 22, 2005
Last modified: February 19, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways