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adk:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

Standard name

Adk

Synonyms

adenylate kinase[1], B0474[2][1], PlsA[2][1], DnaW[2][1], Adk[2][1]

Product description

ADENYL-KIN[2][3]

EC number (for enzymes)
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Notes

Function

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

QualifierGO IDGO term nameReference(s)Evidence Codewith/fromAspectNotesStatus
GO:0000166

nucleotide binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0547

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0004017

adenylate kinase activity

GO_REF:0000002
GO_REF:0000003
GO_REF:0000020

IEA: Inferred from Electronic Annotation

InterPro:IPR007862
EC:2.7.4.3
HAMAP:MF_00235

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005524

ATP binding

GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000004
GO_REF:0000020

IEA: Inferred from Electronic Annotation

InterPro:IPR000850
InterPro:IPR006259
InterPro:IPR011769
SP_KW:KW-0067
HAMAP:MF_00235

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005737

cytoplasm

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0963

C

Seeded from EcoCyc 12.5 [4]

complete

GO:0006139

nucleobase, nucleoside, nucleotide and nucleic acid metabolic process

GO_REF:0000002
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000850
InterPro:IPR006259

P

Seeded from EcoCyc 12.5 [4]

complete

GO:0009165

nucleotide biosynthetic process

GO_REF:0000004
GO_REF:0000020

IEA: Inferred from Electronic Annotation

SP_KW:KW-0545
HAMAP:MF_00235

P

Seeded from EcoCyc 12.5 [4]

complete

GO:0016301

kinase activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0418

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0016740

transferase activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0808

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0016776

phosphotransferase activity, phosphate group as acceptor

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006259

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0019201

nucleotide kinase activity

GO_REF:0000002
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006259
InterPro:IPR011769

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0019205

nucleobase, nucleoside, nucleotide kinase activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000850

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0004017

adenylate kinase activity

PMID:6311616[5]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005515

protein binding

PMID:11106368[6]

IPI: Inferred from Physical Interaction

UniProtKB:P0A7B1

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005515

protein binding

PMID:15690043[7]

IPI: Inferred from Physical Interaction

UniProtKB:P0A8T7

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005515

protein binding

PMID:15690043[7]

IPI: Inferred from Physical Interaction

UniProtKB:P77806

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005524

ATP binding

PMID:10736163[8]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0009152

purine ribonucleotide biosynthetic process

PMID:166976[9]

IMP: Inferred from Mutant Phenotype

P

Seeded from EcoCyc 12.5 [4]

complete

GO:0015951

purine ribonucleotide interconversion

PMID:166976[9]

IMP: Inferred from Mutant Phenotype

P

Seeded from EcoCyc 12.5 [4]

complete

GO:0016208

AMP binding

PMID:10736163[8]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0015949

nucleobase, nucleoside and nucleotide interconversion

P

Seeded from EcoCyc 11.1[3].

required fields missing

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Interactions

Partner TypePartnerNotesReferences
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Notes

Localization

CompartmentDescriptionEvidenceNotes

cytoplasm

From EcoCyc[3]

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Notes

Structure and Physical Properties

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Physical Properties

Sequence

at EcoCyc

MRIILLGAPG AGKGTQAQFI MEKYGIPQIS TGDMLRAAVK SGSELGKQAK DIMDAGKLVT
DELVIALVKE RIAQEDCRNG FLLDGFPRTI PQADAMKEAG INVDYVLEFD VPDELIVDRI
VGRRVHAPSG RVYHVKFNPP KVEGKDDVTG EELTTRKDDQ EETVRKRLVE YHQMTAPLIG
YYSKEAEAGN TKYAKVDGTK PVAEVRADLE KILG
Mol. Wt

23.59 kDa (calc) [2]

pI

5.81[2]

Extinction coefficient

10430 - 10555 (calc based on 7 Y, 0 W, and 1 C residues)

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Domains/Motifs/Modification Sites

TypeResiduesDescriptionNotes
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Structure

Structures
  • Representative Escherichia coli structure:
    1E4V|A
    1-214 of 214 residues (E-value: 2.2e-110) (Percent Identity: 99.53)
  • Representative homolog:
    1QF9|A (Dictyostelium discoideum)
    9-131 of 214 residues (E-value: 1.2e-20) (Percent Identity: 33.87)
  • View all other structures.
Models

View models at:

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Notes

Gene Product Resources

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Resource typeSourceNotes/Reference
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Notes

Accessions in Other Databases

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DatabaseAccessionNotes

EcoCyc (EcoliWiki Page)

EcoCyc:ADENYL-KIN-MONOMER

UniProt (EcoliWiki Page)

UniProt:P69441

PFAM (EcoliWiki Page)

PFAM:PF00406

RefSeq (EcoliWiki Page)

RefSeq:NP_415007

ModBase (EcoliWiki Page)

ModBase:P69441

PDB (EcoliWiki Page)

PDB:1AKE


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Notes

Links

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NameURLComments
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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 1.5 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. 2.0 2.1 2.2 2.3 2.4 2.5 2.6 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. 3.0 3.1 3.2 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. 4.00 4.01 4.02 4.03 4.04 4.05 4.06 4.07 4.08 4.09 4.10 4.11 4.12 4.13 4.14 4.15 4.16 4.17 4.18 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  5. Bârzu O & Michelson S (1983) Simple and fast purification of Escherichia coli adenylate kinase. FEBS Lett 153: 280-4 PubMed EcoliWiki page
  6. Ishige K & Noguchi T (2000) Inorganic polyphosphate kinase and adenylate kinase participate in the polyphosphate:AMP phosphotransferase activity of Escherichia coli. Proc Natl Acad Sci U S A 97: 14168-71 PubMed EcoliWiki page
  7. 7.0 7.1 Butland G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433: 531-7 PubMed EcoliWiki page
  8. 8.0 8.1 Lin Y & Nageswara Rao BD (2000) Structural characterization of adenine nucleotides bound to Escherichia coli adenylate kinase. 2. 31P and 13C relaxation measurements in the presence of cobalt(II) and manganese(II). Biochemistry 39: 3647-55 PubMed EcoliWiki page
  9. 9.0 9.1 Glaser M et al. (1975) Role of adenylate kinase in the regulation of macromolecular biosynthesis in a putative mutant of Escherichia coli defective in membrane phospholipid biosynthesis. J Bacteriol 123: 128-36 PubMed EcoliWiki page


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