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C3TED2 (C3TED2_ECOLX) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 15. 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 1 HAMAP MF_00219
Short name=DHOase 1 HAMAP MF_00219
EC=3.5.2.3 HAMAP MF_00219
Gene names
Name:pyrC1 HAMAP MF_00219
ORF Names:ECs1440 EMBL ACI85066.1
OrganismEscherichia coli EMBL ACI85066.1
Taxonomic identifier562 [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. SAAS SAAS004721 RuleBase RU003440 HAMAP MF_00219

Cofactor

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

Pathway

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

Subunit structure

Homodimer By similarity. SAAS SAAS004721 HAMAP MF_00219

Sequence similarities

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

Sequences

Sequence LengthMass (Da)Tools
C3TED2 [UniParc].

Last modified June 16, 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]"A precise reconstruction of the emergence and constrained radiations of Escherichia coli O157 portrayed by backbone concatenomic analysis."
Leopold S.R., Magrini V., Holt N.J., Shaikh N., Mardis E.R., Cagno J., Ogura Y., Iguchi A., Hayashi T., Mellmann A., Karch H., Besser T.E., Sawyer S.A., Whittam T.S., Tarr P.I.
Proc. Natl. Acad. Sci. U.S.A. 106:8713-8718(2009) [PubMed: 19439656] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 493/89 EMBL ACI85066.1, 86-24 EMBL ACI85067.1, 87-14 EMBL ACI85068.1, TB182A EMBL ACI85069.1 and TW14359 EMBL ACI85070.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		EU902520 Genomic DNA. Translation: ACI85066.1.
EU902521 Genomic DNA. Translation: ACI85067.1.
EU902522 Genomic DNA. Translation: ACI85068.1.
EU902523 Genomic DNA. Translation: ACI85069.1.
EU902524 Genomic DNA. Translation: ACI85070.1.

3D structure databases

ProteinModelPortalC3TED2.
SMRC3TED2. Positions 4-347.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_00219. PyrC_type1.
[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 nameC3TED2_ECOLX
AccessionPrimary (citable) accession number: C3TED2
Entry history
Integrated into UniProtKB/TrEMBL: June 16, 2009
Last sequence update: June 16, 2009
Last modified: January 25, 2012
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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