Skip Header

Contribute Send feedback
Read comments (?) or add your own

B1XF88 (ADD_ECODH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adenosine deaminase
EC=3.5.4.4
Alternative name(s):
Adenosine aminohydrolase
Gene names
Name:add
Ordered Locus Names:ECDH10B_1756
OrganismEscherichia coli (strain K12 / DH10B) [Complete proteome] [HAMAP]
Taxonomic identifier316385 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Adenosine + H2O = inosine + NH3. HAMAP MF_00540

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00540

Sequence similarities

Belongs to the adenosine and AMP deaminases family. Adenosine deaminase subfamily.

Ontologies

Keywords
   Biological processNucleotide metabolism
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpurine ribonucleoside monophosphate biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionadenosine deaminase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 333333Adenosine deaminase HAMAP MF_00540
PRO_1000128843

Sites

Active site2001Proton donor By similarity
Metal binding121Zinc; catalytic By similarity
Metal binding141Zinc; catalytic By similarity
Metal binding1971Zinc; catalytic By similarity
Metal binding2781Zinc; catalytic By similarity
Binding site141Substrate By similarity
Binding site161Substrate By similarity
Binding site1701Substrate; via amide nitrogen and carbonyl oxygen By similarity
Binding site2791Substrate By similarity
Site2211Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
B1XF88 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 6234BBC13C505ED6

FASTA33336,397
        10         20         30         40         50         60 
MIDTTLPLTD IHRHLDGNIR PQTILELGRQ YNISLPAQSL ETLIPHVQVI ANEPDLVSFL 

        70         80         90        100        110        120 
TKLDWGVKVL ASLDACRRVA FENIEDAARH GLHYVELRFS PGYMAMAHQL PVAGVVEAVI 

       130        140        150        160        170        180 
DGVREGCRTF GVQAKLIGIM SRTFGEAACQ QELEAFLAHR DQITALDLAG DELGFPGSLF 

       190        200        210        220        230        240 
LSHFNRARDA GWHITVHAGE AAGPESIWQA IRELGAERIG HGVKAIEDRA LMDFLAEQQI 

       250        260        270        280        290        300 
GIESCLTSNI QTSTVAELAA HPLKTFLEHG IRASINTDDP GVQGVDIIHE YTVAAPAAGL 

       310        320        330 
SREQIRQAQI NGLEMAFLSA EEKRALREKV AAK

« Hide

References

[1]"The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse."
Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B., Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B., Posfai G., Weinstock G.M., Blattner F.R.
J. Bacteriol. 190:2597-2606(2008) [PubMed: 18245285] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / DH10B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000948 Genomic DNA. Translation: ACB02829.1.
RefSeqYP_001730607.1. NC_010473.1.

3D structure databases

ProteinModelPortalB1XF88.
SMRB1XF88. Positions 5-333.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1XF88.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000013266; EBESCP00000012794; EBESCG00000012328.
GeneID6061844.
GenomeReviewsGene locus ECDH10B_1756 in contig CP000948_GR.
KEGGecd:ECDH10B_1756.
PATRIC18463366. VBIEscCol59506_1780.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000009969.
HOGENOMHBG630382.
OMAPYYMAMN.
ProtClustDBPRK09358.

Enzyme and pathway databases

BioCycECOL316385:ECDH10B_1756-MONOMER.

Family and domain databases

HAMAPMF_00540. A_deaminase.
[Tree]
InterProIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006330. A_deaminase.
[Graphical view]
KOK01488.
PfamPF00962. A_deaminase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01430. Aden_deam. 1 hit.
PROSITEPS00485. A_DEAMINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameADD_ECODH
AccessionPrimary (citable) accession number: B1XF88
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 20, 2008
Last modified: January 25, 2012
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents