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Reviewed, UniProtKB/Swiss-Prot Q3YRI2 (PYRC_EHRCJ)

Last modified June 16, 2009. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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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: Ecaj_0639
OrganismEhrlichia canis (strain Jake) [Complete proteome] [HAMAP]
Taxonomic identifier269484 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Ehrlichia

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Protein attributes

Sequence length447 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP MF_00220

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. HAMAP MF_00220

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the DHOase family. Type 2 subfamily.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 447447Dihydroorotase HAMAP MF_00220
PRO_0000325592

Sites

Metal binding811Zinc 1 By similarity
Metal binding831Zinc 1 By similarity
Metal binding1611Zinc 1; via carbamate group By similarity
Metal binding1611Zinc 2; via carbamate group By similarity
Metal binding1981Zinc 2 By similarity
Metal binding2521Zinc 2 By similarity
Metal binding3251Zinc 1 By similarity

Amino acid modifications

Modified residue1611N6-carboxylysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q3YRI2-1 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: 9B695F6620AEBE43

FASTA44749,115
        10         20         30         40         50         60 
MYKQSWKLLG RGQDADFTVA YINARIIDPE SKLDIIGSLL TKGDKIVDFG QDLFNNGIPS 

        70         80         90        100        110        120 
TIDEVVDCNN NILMPGLIDI HVHFREPGQE HKETIHTGSK SAAAGGVTTV VCQPNTIPTI 

       130        140        150        160        170        180 
SSIITAKYIK MRALESAYVN IEFYASITKP DNSLSDMALL KEAGAVGFTD DGMPVMNSLT 

       190        200        210        220        230        240 
MRQALSYSSM LDTVVAQHAE DLNLSNNGHI NEGTVSYELG LKGIPDISES IIVNRDIALM 

       250        260        270        280        290        300 
KNIKNVHYHI LHVSSQDSLN IIKQAKNQGL KVTCEVTPHH LTLTEQDVIT HGTLAKINPP 

       310        320        330        340        350        360 
LRTENDRLSM VEGLKNGIID CIATDHAPHE VNTKELPLDT AAFGIVGLET MLPISLELYH 

       370        380        390        400        410        420 
NGTISLIDLL ATLTYKPANI IKVPRGRIKK GFVADLIILD LNHEWTIDIL KFASKSKNSP 

       430        440 
FHNRKVKGKV LRTIVSGKTT YTAVRNI

« Hide

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References

[1]"The genome of the obligately intracellular bacterium Ehrlichia canis reveals themes of complex membrane structure and immune evasion strategies."
Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P., Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M., Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.
J. Bacteriol. 188:4015-4023(2006) [PubMed: 16707693] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000107 Genomic DNA. Translation: AAZ68673.1.
RefSeqYP_303271.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3618182.
GenomeReviewsGene locus Ecaj_0639 in contig CP000107_GR.
KEGGecn:Ecaj_0639.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ3YRI2.
OMAQ3YRI2. CDVHPVG.

Enzyme and pathway databases

BioCycECAN269484:ECAJ_0639-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...

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Entry information

Entry namePYRC_EHRCJ
AccessionPrimary (citable) accession number: Q3YRI2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: September 27, 2005
Last modified: June 16, 2009
This is version 27 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)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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