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UniProtKB/Swiss-Prot entry P22333


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ADD_ECOLI
Primary accession number P22333
Secondary accession numbers P78163 P78240
Integrated into Swiss-Prot on August 1, 1991
Sequence was last modified on November 1, 1997 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 73)
Name and origin of the protein
Protein name Adenosine deaminase
Synonyms EC 3.5.4.4
Adenosine aminohydrolase
Gene name
Name: add
OrderedLocusNames: b1623, JW1615
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
DOI=10.1021/bi00222a033; PubMed=1998686 [NCBI, ExPASy, EBI, Israel, Japan]
Chang Z., Nygaard P., Chinault A.C., Kellems R.E.;
"Deduced amino acid sequence of Escherichia coli adenosine deaminase reveals evolutionarily conserved amino acid residues: implications for catalytic function.";
Biochemistry 30:2273-2280(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.6.363; PubMed=9097039 [NCBI, ExPASy, EBI, Israel, Japan]
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., Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
"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.";
DNA Res. 3:363-377(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M59033; AAA23419.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC74695.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA15374.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A64919; A64919.
RefSeq AP_002244.1; -.
NP_416140.1; -.
3D structure databases
HSSP P03958; 1A4M. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase P22333.
Protein-protein interaction databases
DIP DIP:9056N; -.
Enzyme and pathway databases
BioCyc EcoCyc:ADENODEAMIN-MON; -.
MetaCyc:ADENODEAMIN-MON; -.
Organism-specific databases
EchoBASE EB0029; -.
EcoGene EG10030; add.
Ontologies
GO
GO:0004000; Molecular function: adenosine deaminase activity (inferred from electronic annotation from HAMAP).
GO:0009168; Biological process: purine ribonucleoside monophosphate biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00540; -; 1.
PBIL [Tree]
InterPro IPR006650; A/AMP_deam_AS.
IPR001365; A/AMP_deaminase.
IPR006330; A_deaminase.
Graphical view of domain structure.
PANTHER PTHR11409; A/AMP_deaminase; 1.
Pfam PF00962; A_deaminase; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01430; aden_deam; 1.
PROSITE PS00485; A_DEAMINASE; 1.
ProtoNet P22333.
Genome annotation databases
GeneID 945851; -.
GenomeReviews U00096_GR; b1623.
AP009048_GR; JW1615.
KEGG ecj:JW1615; -.
eco:b1623; -.
Phylogenomic databases
HOGENOM P22333; -.
Genome annotation databases
CMR P22333; b1623.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Hydrolase; Nucleotide metabolism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   333  333     Adenosine deaminase. PRO_0000194367
ACT_SITE   197   197        Potential. 
ACT_SITE   245   245        Potential. 
ACT_SITE   278   278        Potential. 
ACT_SITE   279   279        Potential. 
CONFLICT   145   145        Missing (in Ref. 1; AAA23419). 
Sequence information
Length: 333 AA [This is the length of the unprocessed precursor] Molecular weight: 36397 Da [This is the MW of the unprocessed precursor] CRC64: 6234BBC13C505ED6 [This is a checksum on the sequence]
        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 

P22333 in FASTA format

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