Skip Header

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

B1IQD2 (ADD_ECOLC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. 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:EcolC_2007
OrganismEscherichia coli (strain ATCC 8739 / DSM 1576 / Crooks) [Complete proteome] [HAMAP]
Taxonomic identifier481805 [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_1000081923

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
B1IQD2 [UniParc].

Last modified April 29, 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]"Complete sequence of Escherichia coli C str. ATCC 8739."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Ingram L., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 8739 / DSM 1576 / Crooks.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000946 Genomic DNA. Translation: ACA77653.1.
RefSeqYP_001724980.1. NC_010468.1.

3D structure databases

ProteinModelPortalB1IQD2.
SMRB1IQD2. Positions 5-333.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1IQD2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000008876; EBESCP00000008560; EBESCG00000007939.
GeneID6068080.
GenomeReviewsGene locus EcolC_2007 in contig CP000946_GR.
KEGGecl:EcolC_2007.
PATRIC18226866. VBIEscCol82905_2156.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000009969.
HOGENOMHBG630382.
OMAPYYMAMN.
ProtClustDBPRK09358.

Enzyme and pathway databases

BioCycECOL481805:ECOLC_2007-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_ECOLC
AccessionPrimary (citable) accession number: B1IQD2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 29, 2008
Last modified: January 25, 2012
This is version 28 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