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C6UR10 (C6UR10_ECO5T) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydroorotase HAMAP MF_00219
Short name=DHOase HAMAP MF_00219
EC=3.5.2.3 HAMAP MF_00219
Gene names
Name:pyrC HAMAP MF_00219 EMBL ACT71205.1
Ordered Locus Names:ECSP_1363
OrganismEscherichia coli O157:H7 (strain TW14359 / EHEC) [Complete proteome] [HAMAP]
Taxonomic identifier544404 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP MF_00219 RuleBase RU003440 SAAS SAAS004721

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP MF_00219 RuleBase RU003440 SAAS SAAS004721

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP MF_00219 RuleBase RU003440 SAAS SAAS004721

Subunit structure

Homodimer By similarity. HAMAP MF_00219 SAAS SAAS004721

Sequence similarities

Belongs to the DHOase family. Type 1 subfamily. HAMAP MF_00219 RuleBase RU003440

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Metal binding171Zinc 1 By similarity HAMAP MF_00219
Metal binding191Zinc 1 By similarity HAMAP MF_00219
Metal binding1031Zinc 1; via carbamate group By similarity HAMAP MF_00219
Metal binding1031Zinc 2; via carbamate group By similarity HAMAP MF_00219
Metal binding1401Zinc 2 By similarity HAMAP MF_00219
Metal binding1781Zinc 2 By similarity HAMAP MF_00219
Metal binding2511Zinc 1 By similarity HAMAP MF_00219

Amino acid modifications

Modified residue1031N6-carboxylysine By similarity HAMAP MF_00219

Sequences

Sequence LengthMass (Da)Tools
C6UR10 [UniParc].

Last modified September 22, 2009. Version 1.
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

[1]"Analysis of the genome of the Escherichia coli O157:H7 2006 spinach-associated outbreak isolate indicates candidate genes that may enhance virulence."
Kulasekara B.R., Jacobs M., Zhou Y., Wu Z., Sims E., Saenphimmachak C., Rohmer L., Ritchie J.M., Radey M., McKevitt M., Freeman T.L., Hayden H., Haugen E., Gillett W., Fong C., Chang J., Beskhlebnaya V., Waldor M.K. expand/collapse author list , Samadpour M., Whittam T.S., Kaul R., Brittnacher M., Miller S.I.
Infect. Immun. 77:3713-3721(2009) [PubMed: 19564389] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001368 Genomic DNA. Translation: ACT71205.1.
RefSeqYP_003077281.1. NC_013008.1.

3D structure databases

ProteinModelPortalC6UR10.
SMRC6UR10. Positions 4-347.
ModBaseSearch...

Protein-protein interaction databases

STRINGC6UR10.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000169120; EBESCP00000159680; EBESCG00000164599.
GeneID8215929.
GenomeReviewsGene locus ECSP_1363 in contig CP001368_GR.
KEGGetw:ECSP_1363.
PATRIC18386634. VBIEscCol9396_1375.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000011208.
OMACLPVAKR.
ProtClustDBPRK05451.

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 nameC6UR10_ECO5T
AccessionPrimary (citable) accession number: C6UR10
Entry history
Integrated into UniProtKB/TrEMBL: September 22, 2009
Last sequence update: September 22, 2009
Last modified: December 14, 2011
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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