add:Gene Product(s): Difference between revisions

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|-
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!align=left {{table heading style}} |Standard name
!align=left |Standard name
||
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Add  
Add  
|-
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!align=left {{table heading style}} |Synonyms
!align=left |Synonyms
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adenosine deaminase<ref name='LIB:Riley_2006'/>, B1623<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Add<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>  
adenosine deaminase<ref name='LIB:Riley_2006'/>, B1623<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Add<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>  
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!align=left {{table heading style}} |Product description
!align=left |Product description
||
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Adenosine deaminase; mutants affect growth on deoxyadenosine in purA, B mutants<ref name='LIB:EcoGene'/>
Adenosine deaminase; mutants affect growth on deoxyadenosine in purA, B mutants<ref name='LIB:EcoGene'/>
|-
|-
!align=left {{table heading style}} |EC number (for enzymes)
!align=left |EC number (for enzymes)
||
||
* [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.4 3.5.4.4]<ref name='LIB:Riley_2006'/>
* [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.4 3.5.4.4]<ref name='LIB:Riley_2006'/>


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!|Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
!|Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
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complete  
complete  


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!|Compartment!!Description!!Evidence!!Source!!Notes
!|Compartment!!Description!!Evidence!!Source!!Notes


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|-
|-
!align=left {{table heading style}} |Sequence
!align=left |Sequence
||
||
[http://biocyc.org/ECOLI/sequence-aa?object=ADENODEAMIN-MONOMER at EcoCyc]  
[http://biocyc.org/ECOLI/sequence-aa?object=ADENODEAMIN-MONOMER at EcoCyc]  
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SREQIRQAQI NGLEMAFLSA EEKRALREKV AAK</pre>  
SREQIRQAQI NGLEMAFLSA EEKRALREKV AAK</pre>  
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!align=left {{table heading style}} |Length
!align=left |Length
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333
333
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!align=left {{table heading style}} |Mol. Wt
!align=left |Mol. Wt
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36.397 kDa
36.397 kDa
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!align=left {{table heading style}} |pI
!align=left |pI
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5.4 (calculated)
5.4 (calculated)
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!align=left {{table heading style}} |Extinction coefficient
!align=left |Extinction coefficient
||
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22,460 - 22,960 (calc based on 4 Y, 3 W, and 4 C residues)
22,460 - 22,960 (calc based on 4 Y, 3 W, and 4 C residues)


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<beststructure>
<beststructure>
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</beststructure>
</beststructure>
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!align=left |Models
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View models at:
View models at:
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* [http://spock.genes.nig.ac.jp/~genome/search.html Genomes TO Protein] (GTOP)
* [http://spock.genes.nig.ac.jp/~genome/search.html Genomes TO Protein] (GTOP)


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Revision as of 23:54, 8 January 2010

{{#css:Suppresslinks.css}}<css>h1 .editsection { display:none;} h2 .editsection { display:none;}</css>

Quickview   Gene   Gene Product(s)   Expression   Evolution   On One Page    
Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

Add

Synonyms

adenosine deaminase[1], B1623[2][1], Add[2][1]

Product description

Adenosine deaminase; mutants affect growth on deoxyadenosine in purA, B mutants[3]

EC number (for enzymes)
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Notes

Adenosine deaminase is the enzyme that catalyzes the irreversible deamination of adenosine or deoxyadenosine to inosine or deoxyinosine. The active site of ADA contains residues of a Histidine, 2 Aspartic acids, one Glutamic acid, and a zinc atom. The overall mechanism involves a hydroxyl group addition to C6 of adenosine, which forms the tetrahedral transition state intermediate. Then, the ammonia elimination forms inosine. Zinc acts as a powerful electrophile, which allows a water molecule to attack C6. Glutamic acid interacts with N1 and donates a proton, reducing the N1=C6 double bond character, allowing the hydroxyl nucleophilic attack. A Histidine residue and the carboxylic group of aspartic acid stabilizes and orients the zinc-bound water molecule. The ammonia elimination pathway is not quite understood but is the final step in the mechanism of adenosine deaminase.

Function

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Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference(s) Evidence Code with/from Aspect Notes Status
GO:0016787

hydrolase activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0378

F

Seeded from EcoCyc [4]

complete

GO:0009168

purine ribonucleoside monophosphate biosynthetic process

GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000020

IEA: Inferred from Electronic Annotation

InterPro:IPR001365
InterPro:IPR006330
InterPro:IPR006650
HAMAP:MF_00540

P

Seeded from EcoCyc 12.5 [5]

complete

GO:0009117

nucleotide metabolic process

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0546

P

Seeded from EcoCyc [4]

complete

GO:0004000

adenosine deaminase activity

GO_REF:0000002
GO_REF:0000003
GO_REF:0000020

IEA: Inferred from Electronic Annotation

InterPro:IPR006330
EC:3.5.4.4
HAMAP:MF_00540

F

Seeded from EcoCyc 12.5 [5]

complete

GO:0019239

deaminase activity

GO_REF:0000002
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001365
InterPro:IPR006650

F

Seeded from EcoCyc [4]

complete

GO:0005737

cytoplasm

C

Seeded from Riley et al 2006 [1].

required fields missing

GO:0015949

nucleobase, nucleoside and nucleotide interconversion

P

Seeded from EcoCyc 11.1[6].

required fields missing

GO:0004000

adenosine deaminase activity

PMID:4874315[7]

IDA: Inferred from Direct Assay

F

complete

GO:0004000

adenosine deaminase activity

PMID:765747[8]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0015950

purine nucleotide interconversion

PMID:1998686[9]

IGI: Inferred from Genetic Interaction

EcoliWiki:guaA


P

complete

GO:0009168

purine ribonucleoside monophosphate biosynthetic process

PMID:1998686[9]

IGI: Inferred from Genetic Interaction

EcoliWiki:guaA


P

complete

GO:0005488

binding

PMID:3486673[10]

ISS: Inferred from Sequence or Structural Similarity

UniProtKB:P56658

F

CHEBI:27834 (Deoxycoformycin mechanistically inhibits Add).

complete

GO:0006154

adenosine catabolic process

PMID:1998686[9]

IGI: Inferred from Genetic Interaction

EcoliWiki:guaA


P

complete

GO:0004000

adenosine deaminase activity

PMID:5335916[11]

IDA: Inferred from Direct Assay

F

complete

GO:0032261

purine nucleotide salvage

PMID:1998686[9]

IGI: Inferred from Genetic Interaction

EcoliWiki:guaA


P

complete

GO:0043103

hypoxanthine salvage

PMID:1998686[9]

IGI: Inferred from Genetic Interaction

EcoliWiki:guaA


P

complete

GO:0046101

hypoxanthine biosynthetic process

PMID:1998686[9]

IGI: Inferred from Genetic Interaction

EcoliWiki:guaA


P

complete

GO:0005737

cytoplasm

PMID:5335916[11]

IC: Inferred by Curator

C

complete

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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence

Protein

rpsM

PMID:16606699[12]

Experiment(s):EBI-1140315

Protein

arpA

PMID:16606699[12]

Experiment(s):EBI-1140315

Protein

rplT

PMID:16606699[12]

Experiment(s):EBI-1140315

Protein

insC1

PMID:16606699[12]

Experiment(s):EBI-1140315

Protein

ligA

PMID:16606699[12]

Experiment(s):EBI-1140315

Protein

gcd

PMID:16606699[12]

Experiment(s):EBI-1140315

Small Molecule

CHEBI:27834 (Deoxycoformycin)

Inhibitor of Add activity


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Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Source Notes
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Notes

Structure and Physical Properties

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Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Sequence

at EcoCyc 

MIDTTLPLTD IHRHLDGNIR PQTILELGRQ YNISLPAQSL ETLIPHVQVI ANEPDLVSFL
TKLDWGVKVL ASLDACRRVA FENIEDAARH GLHYVELRFS PGYMAMAHQL PVAGVVEAVI
DGVREGCRTF GVQAKLIGIM SRTFGEAACQ QELEAFLAHR DQITALDLAG DELGFPGSLF
LSHFNRARDA GWHITVHAGE AAGPESIWQA IRELGAERIG HGVKAIEDRA LMDFLAEQQI
GIESCLTSNI QTSTVAELAA HPLKTFLEHG IRASINTDDP GVQGVDIIHE YTVAAPAAGL
SREQIRQAQI NGLEMAFLSA EEKRALREKV AAK
Length

333

Mol. Wt

36.397 kDa

pI

5.4 (calculated)

Extinction coefficient

22,460 - 22,960 (calc based on 4 Y, 3 W, and 4 C residues)

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Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes
edit table

<motif_map/>

Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=add taxon=562,83333 </beststructure>

Models

View models at:

edit table

Structure figures

Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

EcoCyc (EcoliWiki Page)

EcoCyc:ADENODEAMIN-MONOMER

UniProt (EcoliWiki Page)

UniProt:P22333

PFAM (EcoliWiki Page)

PFAM:PF00962

RefSeq (EcoliWiki Page)

RefSeq:NP_416140


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Notes

Links

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References

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See Help:References for how to manage references in EcoliWiki.

  1. ↑ 1.0 1.1 1.2 1.3 1.4 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  4. ↑ 4.0 4.1 4.2 EcoCyc (release 13.0; 2009) Keseler, IM et al. (2009) Nucleic Acids Res. 37(Database issue):D464-70
  5. ↑ 5.0 5.1 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  6. ↑ EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  7. ↑ Remy, CN & Love, SH (1968) Induction of adenosine deaminase in Escherichia coli. J. Bacteriol. 96 76-85 PubMed
  8. ↑ Jochimsen, B et al. (1975) Location on the chromosome of Escherichia coli of genes governing purine metabolism. Adenosine deaminase (add), guanosine kinase (gsk) and hypoxanthine phosphoribosyltransferase (hpt). Mol. Gen. Genet. 143 85-91 PubMed
  9. ↑ 9.0 9.1 9.2 9.3 9.4 9.5 Chang, ZY et al. (1991) Deduced amino acid sequence of Escherichia coli adenosine deaminase reveals evolutionarily conserved amino acid residues: implications for catalytic function. Biochemistry 30 2273-80 PubMed
  10. ↑ Frick, L et al. (1986) Transition-state stabilization by adenosine deaminase: structural studies of its inhibitory complex with deoxycoformycin. Biochemistry 25 1616-21 PubMed
  11. ↑ 11.0 11.1 Wolfenden, R et al. (1967) Substrate binding by adenosine deaminase. Specificity, pH dependence, and competition by mercurials. J. Biol. Chem. 242 977-83 PubMed
  12. ↑ 12.0 12.1 12.2 12.3 12.4 12.5 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed

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