ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P28248


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name DCD_ECOLI
Primary accession number P28248
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on December 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 69)
Name and origin of the protein
Protein name Deoxycytidine triphosphate deaminase
Synonyms dCTP deaminase
EC 3.5.4.13
Gene name
Name: dcd
Synonyms: dus, paxA
OrderedLocusNames: b2065, JW2050
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
STRAIN=K12;
PubMed=1324907 [NCBI, ExPASy, EBI, Israel, Japan]
Wang L., Weiss B.;
"dcd (dCTP deaminase) gene of Escherichia coli: mapping, cloning, sequencing, and identification as a locus of suppressors of lethal dut (dUTPase) mutations.";
J. Bacteriol. 174:5647-5653(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.6.379; PubMed=9097040 [NCBI, ExPASy, EBI, Israel, Japan]
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.;
"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map.";
DNA Res. 3:379-392(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M90069; AAA23669.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75126.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA15918.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A42940; A42940.
RefSeq AP_002665.1; -.
NP_416569.1; -.
3D structure databases
PDB
1XS1; X-ray; 1.80 A; A/B/C/D/E/F=1-193.[ExPASy / RCSB / EBI]
1XS4; X-ray; 2.53 A; A/B/C/D/E/F=1-193.[ExPASy / RCSB / EBI]
1XS6; X-ray; 2.00 A; A/B/C/D/E/F=1-193.[ExPASy / RCSB / EBI]
2J4H; X-ray; 2.70 A; A/B=1-193.[ExPASy / RCSB / EBI]
2J4Q; X-ray; 2.60 A; A/B=1-193.[ExPASy / RCSB / EBI]
2V9X; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-193.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1XS1; -.
1XS4; -.
1XS6; -.
2J4H; -.
2J4Q; -.
2V9X; -.
ModBase P28248.
Protein-protein interaction databases
IntAct P28248; -.
Enzyme and pathway databases
BioCyc EcoCyc:DCTP-DEAM-MON; -.
MetaCyc:DCTP-DEAM-MON; -.
Organism-specific databases
EchoBASE EB1389; -.
EcoGene EG11418; dcd.
Ontologies
GO
GO:0008829; Molecular function: dCTP deaminase activity (inferred from electronic annotation from HAMAP).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006229; Biological process: dUTP biosynthetic process (inferred from electronic annotation from InterPro).
GO:0009220; Biological process: pyrimidine ribonucleotide biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00146; -; 1.
PBIL [Tree]
InterPro IPR011962; dCTP_deam.
IPR008180; DeoxyUTPase.
Graphical view of domain structure.
Pfam PF00692; dUTPase; 1.
Pfam graphical view of domain structure.
ProDom PD004900; dCTP_deaminase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR02274; dCTP_deam; 1.
BLOCKS P28248.
ProtoNet P28248.
Genome annotation databases
GeneID 946593; -.
GenomeReviews U00096_GR; b2065.
AP009048_GR; JW2050.
KEGG ecj:JW2050; -.
eco:b2065; -.
Phylogenomic databases
HOGENOM P28248; -.
Genome annotation databases
CMR P28248; b2065.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Direct protein sequencing; Hydrolase; Nucleotide metabolism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   193  193     Deoxycytidine triphosphate deaminase. PRO_0000155984
HELIX   5    14  10      
STRAND   15    21  7      
HELIX   25    27  3      
STRAND   32    37  6      
STRAND   39    42  4      
HELIX   46    48  3      
HELIX   58    68  11      
STRAND   81    83  3      
STRAND   89    98  10      
STRAND   103   108  6      
HELIX   111   114  4      
TURN   115   117  3      
STRAND   118   120  3      
STRAND   132   141  10      
STRAND   143   145  3      
STRAND   147   149  3      
STRAND   153   162  10      
HELIX   171   173  3      
STRAND   180   182  3      
HELIX   190   192  3      
Sequence information
Length: 193 AA [This is the length of the unprocessed precursor] Molecular weight: 21249 Da [This is the MW of the unprocessed precursor] CRC64: B0044051ADE7F919 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRLCDRDIEA WLDEGRLSIN PRPPVERING ATVDVRLGNK FRTFRGHTAA FIDLSGPKDE 

        70         80         90        100        110        120 
VSAALDRVMS DEIVLDEGEA FYLHPGELAL AVTLESVTLP ADLVGWLDGR SSLARLGLMV 

       130        140        150        160        170        180 
HVTAHRIDPG WSGCIVLEFY NSGKLPLALR PGMLIGALSF EPLSGPAVRP YNRREDAKYR 

       190 
NQQGAVASRI DKD 

P28248 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by au flag APAF Australia Mirror sites: Brazil  Canada  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!