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Reviewed, UniProtKB/Swiss-Prot Q8X8N8 (PYRC_ECO57)

Last modified November 25, 2008. Version 50. 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

Names and origin

Protein namesRecommended name:
    Dihydroorotase
      Short name=DHOase
    EC=3.5.2.3
Gene names
Name: pyrC
Ordered Locus Names: Z1699, ECs1440
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 348347Dihydroorotase
PRO_0000147207

Sites

Metal binding171Zinc 1 By similarity
Metal binding191Zinc 1 By similarity
Metal binding1031Zinc 1; via carbamate group By similarity
Metal binding1031Zinc 2; via carbamate group By similarity
Metal binding1401Zinc 2 By similarity
Metal binding1781Zinc 2 By similarity
Metal binding2511Zinc 1 By similarity

Amino acid modifications

Modified residue1031N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8X8N8-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 057D1F6834446CA7

FASTA34838,844
        10         20         30         40         50         60 
MTAPSQVLKI RRPDDWHLHL RDGDMLKTVV PYTSEIYGRA IVMPNLAPPV TTVEAAVAYR 

        70         80         90        100        110        120 
QRILHAVPAG HDFTPLMTCY LTDSLDPNEL ERGFNEGVFT AAKLYPANAT TNSSHGVTSV 

       130        140        150        160        170        180 
DAIMPVLERM EKIGMPLLVH GEVTHADIDI FDREARFIES VMEPLRQRLT ALKVVFEHIT 

       190        200        210        220        230        240 
TKDAADYVRD GNERLAATIT PQHLMFNRNH MLVGGVRPHL YCLPILKRNI HQQALRELVA 

       250        260        270        280        290        300 
SGFNRVFLGT DSAPHARHRK ESSCGCAGCF NAPTALGSYA TVFEEMNALQ HFEAFCSVNG 

       310        320        330        340 
PQFYGLPVND TFIELVREEH QVAESIALTD DTLVPFLAGE TVRWSVKQ 

« Hide

References

Cross-references

Sequence databases

AE005174 Genomic DNA. Translation: AAG55808.1.
BA000007 Genomic DNA. Translation: BAB34863.1.
PIRD85668.
H90808.
RefSeqNP_287196.1.
NP_309467.1.

3D structure databases

HSSPHSSP built from PDB template 1J79 based on UniProtKB P05020.
SMRQ8X8N8. Positions 5-347.
ModBaseSearch...

Genome annotation databases

GeneID914110.
959400.
GenomeReviewsGene locus ECs1440 in contig BA000007_GR.
Gene locus Z1699 in contig AE005174_GR.
KEGGece:Z1699.
ecs:ECs1440.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8X8N8.

Enzyme and pathway databases

BioCycECOL83334:ECS1440-MON.

Family and domain databases

HAMAPMF_00219.
[Tree]
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_ECO57
AccessionPrimary (citable) accession number: Q8X8N8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: January 23, 2007
Last modified: November 25, 2008
This is version 50 of the entry and version 3 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

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