Skip Header

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

A7ZM83 (ADD_ECO24) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. 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

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:EcE24377A_1831
OrganismEscherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]
Taxonomic identifier331111 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

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_1000061054

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
A7ZM83 [UniParc].

Last modified October 23, 2007. 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 pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E24377A / ETEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000800 Genomic DNA. Translation: ABV16769.1.
RefSeqYP_001462912.1. NC_009801.1.

3D structure databases

ProteinModelPortalA7ZM83.
SMRA7ZM83. Positions 5-333.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7ZM83.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000021859; EBESCP00000020921; EBESCG00000020913.
GeneID5587676.
GenomeReviewsGene locus EcE24377A_1831 in contig CP000800_GR.
KEGGecw:EcE24377A_1831.
PATRIC18292925. VBIEscCol31211_2118.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1816.
GeneTreeEBGT00050000009969.
HOGENOMHBG630382.
OMAPYYMAMN.
ProtClustDBPRK09358.

Enzyme and pathway databases

BioCycECOL331111:ECE24377A_1831-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_ECO24
AccessionPrimary (citable) accession number: A7ZM83
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: January 25, 2012
This is version 31 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