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Protein

Adenosine deaminase

Gene

add

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

Adenosine + H2O = inosine + NH3.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi12 – 121Zinc; catalyticUniRule annotation
Metal bindingi14 – 141Zinc; catalyticUniRule annotation
Binding sitei14 – 141SubstrateUniRule annotation
Binding sitei16 – 161SubstrateUniRule annotation
Binding sitei170 – 1701Substrate; via amide nitrogen and carbonyl oxygenUniRule annotation
Metal bindingi197 – 1971Zinc; catalyticUniRule annotation
Active sitei200 – 2001Proton donorUniRule annotation
Sitei221 – 2211Important for catalytic activityUniRule annotation
Metal bindingi278 – 2781Zinc; catalyticUniRule annotation
Binding sitei279 – 2791SubstrateUniRule annotation

GO - Molecular functioni

  • adenosine deaminase activity Source: EcoliWiki
  • zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  • adenosine catabolic process Source: EcoliWiki
  • cellular response to DNA damage stimulus Source: EcoliWiki
  • hypoxanthine biosynthetic process Source: EcoliWiki
  • hypoxanthine salvage Source: EcoliWiki
  • inosine biosynthetic process Source: GO_Central
  • purine nucleotide interconversion Source: EcoliWiki
  • purine nucleotide salvage Source: EcoliWiki
  • purine ribonucleoside monophosphate biosynthetic process Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:ADENODEAMIN-MONOMER.
ECOL316407:JW1615-MONOMER.
MetaCyc:ADENODEAMIN-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenosine deaminaseUniRule annotation (EC:3.5.4.4UniRule annotation)
Alternative name(s):
Adenosine aminohydrolaseUniRule annotation
Gene namesi
Name:addUniRule annotation
Ordered Locus Names:b1623, JW1615
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10030. add.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 333333Adenosine deaminasePRO_0000194367Add
BLAST

Proteomic databases

PaxDbiP22333.
PRIDEiP22333.

Interactioni

Protein-protein interaction databases

DIPiDIP-9056N.
IntActiP22333. 15 interactions.
MINTiMINT-1298977.
STRINGi511145.b1623.

Structurei

3D structure databases

ProteinModelPortaliP22333.
SMRiP22333. Positions 7-326.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1816.
HOGENOMiHOG000218815.
InParanoidiP22333.
KOiK01488.
OMAiDWMVAVL.
OrthoDBiEOG6BPDDD.
PhylomeDBiP22333.

Family and domain databases

HAMAPiMF_00540. A_deaminase.
InterProiIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR028893. A_deaminase.
IPR006330. Ado/ade_deaminase.
[Graphical view]
PfamiPF00962. A_deaminase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01430. aden_deam. 1 hit.
PROSITEiPS00485. A_DEAMINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22333-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIDTTLPLTD IHRHLDGNIR PQTILELGRQ YNISLPAQSL ETLIPHVQVI
60 70 80 90 100
ANEPDLVSFL TKLDWGVKVL ASLDACRRVA FENIEDAARH GLHYVELRFS
110 120 130 140 150
PGYMAMAHQL PVAGVVEAVI DGVREGCRTF GVQAKLIGIM SRTFGEAACQ
160 170 180 190 200
QELEAFLAHR DQITALDLAG DELGFPGSLF LSHFNRARDA GWHITVHAGE
210 220 230 240 250
AAGPESIWQA IRELGAERIG HGVKAIEDRA LMDFLAEQQI GIESCLTSNI
260 270 280 290 300
QTSTVAELAA HPLKTFLEHG IRASINTDDP GVQGVDIIHE YTVAAPAAGL
310 320 330
SREQIRQAQI NGLEMAFLSA EEKRALREKV AAK
Length:333
Mass (Da):36,397
Last modified:November 1, 1997 - v2
Checksum:i6234BBC13C505ED6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451Missing in AAA23419 (PubMed:1998686).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59033 Genomic DNA. Translation: AAA23419.1.
U00096 Genomic DNA. Translation: AAC74695.1.
AP009048 Genomic DNA. Translation: BAA15374.1.
PIRiA64919.
RefSeqiNP_416140.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC74695; AAC74695; b1623.
BAA15374; BAA15374; BAA15374.
GeneIDi945851.
KEGGiecj:Y75_p1599.
eco:b1623.
PATRICi32118548. VBIEscCol129921_1694.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59033 Genomic DNA. Translation: AAA23419.1.
U00096 Genomic DNA. Translation: AAC74695.1.
AP009048 Genomic DNA. Translation: BAA15374.1.
PIRiA64919.
RefSeqiNP_416140.1. NC_000913.3.

3D structure databases

ProteinModelPortaliP22333.
SMRiP22333. Positions 7-326.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-9056N.
IntActiP22333. 15 interactions.
MINTiMINT-1298977.
STRINGi511145.b1623.

Proteomic databases

PaxDbiP22333.
PRIDEiP22333.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74695; AAC74695; b1623.
BAA15374; BAA15374; BAA15374.
GeneIDi945851.
KEGGiecj:Y75_p1599.
eco:b1623.
PATRICi32118548. VBIEscCol129921_1694.

Organism-specific databases

EchoBASEiEB0029.
EcoGeneiEG10030. add.

Phylogenomic databases

eggNOGiCOG1816.
HOGENOMiHOG000218815.
InParanoidiP22333.
KOiK01488.
OMAiDWMVAVL.
OrthoDBiEOG6BPDDD.
PhylomeDBiP22333.

Enzyme and pathway databases

BioCyciEcoCyc:ADENODEAMIN-MONOMER.
ECOL316407:JW1615-MONOMER.
MetaCyc:ADENODEAMIN-MONOMER.

Miscellaneous databases

PROiP22333.

Family and domain databases

HAMAPiMF_00540. A_deaminase.
InterProiIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR028893. A_deaminase.
IPR006330. Ado/ade_deaminase.
[Graphical view]
PfamiPF00962. A_deaminase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01430. aden_deam. 1 hit.
PROSITEiPS00485. A_DEAMINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Deduced amino acid sequence of Escherichia coli adenosine deaminase reveals evolutionarily conserved amino acid residues: implications for catalytic function."
    Chang Z., Nygaard P., Chinault A.C., Kellems R.E.
    Biochemistry 30:2273-2280(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Entry informationi

Entry nameiADD_ECOLI
AccessioniPrimary (citable) accession number: P22333
Secondary accession number(s): P78163, P78240
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: November 1, 1997
Last modified: June 24, 2015
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.