Adenosine deaminase - Escherichia coli (strain K12)

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P22333 (ADD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 113. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Adenosine deaminase
EC=3.5.4.4

Alternative name(s):
Adenosine aminohydrolase

Gene names

Name:	add
Ordered Locus Names:	b1623, JW1615

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	333 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Adenosine + H₂O = inosine + NH₃. HAMAP-Rule MF_00540
Cofactor	Binds 1 zinc ion per subunit By similarity.
Sequence similarities	Belongs to the adenosine and AMP deaminases family. Adenosine deaminase subfamily.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adenosine catabolic process Inferred from genetic interaction Ref.1. Source: EcoliWiki hypoxanthine salvage Inferred from genetic interaction Ref.1. Source: EcoliWiki inosine biosynthetic process Inferred from Biological aspect of Ancestor. Source: RefGenome purine nucleotide interconversion Inferred from genetic interaction Ref.1. Source: EcoliWiki purine nucleotide salvage Inferred from genetic interaction Ref.1. Source: EcoliWiki purine ribonucleoside monophosphate biosynthetic process Inferred from genetic interaction Ref.1. Source: EcoliWiki response to DNA damage stimulus Inferred from expression pattern PubMed 11967071. Source: EcoliWiki
Cellular_component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	adenosine deaminase activity Inferred from direct assay PubMed 4874315 PubMed 5335916. Source: EcoliWiki zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 333

333

Adenosine deaminase HAMAP-Rule MF_00540

PRO_0000194367

Sites

Active site

200

Proton donor By similarity

Metal binding

Zinc; catalytic By similarity

Metal binding

Zinc; catalytic By similarity

Metal binding

197

Zinc; catalytic By similarity

Metal binding

278

Zinc; catalytic By similarity

Binding site

Substrate By similarity

Binding site

Substrate By similarity

Binding site

170

Substrate; via amide nitrogen and carbonyl oxygen By similarity

Binding site

279

Substrate By similarity

Site

221

Important for catalytic activity By similarity

Experimental info

Sequence conflict

145

Missing in AAA23419. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P22333 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 6234BBC13C505ED6
Show »

FASTA

333

36,397

        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

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. Horiuchi T. DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M59033 Genomic DNA. Translation: AAA23419.1. U00096 Genomic DNA. Translation: AAC74695.1. AP009048 Genomic DNA. Translation: BAA15374.1.
PIR	A64919.
RefSeq	NP_416140.1. NC_000913.2. YP_489886.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P22333.
SMR	P22333. Positions 7-326.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-9056N.
IntAct	P22333. 14 interactions.
MINT	MINT-1298977.
STRING	511145.b1623.
Proteomic databases
PaxDb	P22333.
PRIDE	P22333.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC74695; AAC74695; b1623. BAA15374; BAA15374; BAA15374.
GeneID	12931257. 945851.
KEGG	ecj:Y75_p1599. eco:b1623.
PATRIC	32118548. VBIEscCol129921_1694.
Organism-specific databases
EchoBASE	EB0029.
EcoGene	EG10030. add.
Phylogenomic databases
eggNOG	COG1816.
HOGENOM	HOG000218815.
KO	K01488.
OMA	PYYMAMN.
ProtClustDB	PRK09358.
Enzyme and pathway databases
BioCyc	EcoCyc:ADENODEAMIN-MONOMER. ECOL316407:JW1615-MONOMER. MetaCyc:ADENODEAMIN-MONOMER.
Gene expression databases
Genevestigator	P22333.
Family and domain databases
HAMAP	MF_00540. A_deaminase.
InterPro	IPR006650. A/AMP_deam_AS. IPR001365. A/AMP_deaminase_dom. IPR006330. Ado/ade_deaminase. [Graphical view]
Pfam	PF00962. A_deaminase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01430. aden_deam. 1 hit.
PROSITE	PS00485. A_DEAMINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ADD_ECOLI

Accession

Primary (citable) accession number: P22333
Secondary accession number(s): P78163, P78240

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents