adk adenylate kinase [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Gene symbol: adk
Gene description: adenylate kinase
Primary source: ASAP:ABE-0001645
Locus tag: b0474
See related: ECOCYC:EG10032
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage: Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as: dnaW; ECK0468; plsA
Summary: Adenylate kinase is an essential enzyme required for the biosynthesis of purine ribonucleotides and has a key role in controlling the rate of cell growth . [More information is available at EcoCyc: EG10032].
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Genomic context

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Sequence:: NC_000913.3 (497175..497819)

NC_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Adenylate kinase (ADK) conformations segregate naturally into open; intermediate; and closed forms with long-term residence in the intermediate state.
Title: Fine structure of conformational ensembles in adenylate kinase.
These results are consistent with an induced-fit model in which the transition of AdK from an open state to a closed state is initiated by ATP binding.
Title: Effects of Catalytic Action and Ligand Binding on Conformational Ensembles of Adenylate Kinase.
Fast closure of N-terminal long loops but slow formation of beta strands precedes the folding transition state of Escherichia coli adenylate kinase.
Title: Fast closure of N-terminal long loops but slow formation of β strands precedes the folding transition state of Escherichia coli adenylate kinase.
As both open and closed states sampled a wide range of conformation transitions, our simulation strongly supported the conformational selection mechanism for Escherichia coli ADK.
Title: Molecular dynamics studies on the conformational transitions of adenylate kinase: a computational evidence for the conformational selection mechanism.
fast subdomain folding prior to global refolding transition of adenylate kinase; applied double kinetics method to test the hypothesis that specific short native-like intramolecular distances between residues separated by long chain segments in a globular protein can be formed in the collapsed state, prior to the cooperative folding transition
Title: Fast subdomain folding prior to the global refolding transition of E. coli adenylate kinase: a double kinetics study.
In Cartesian space, LID domain closure precedes NMP domain closure in the bound simulation, consistent with prior coarse-grained models of the adenylate kinase conformational transition.
Title: Many local motions cooperate to produce the adenylate kinase conformational transition.
Results demonstrate that the conformational ensemble of adenylate kinase is significantly populated by a locally unfolded state and that the excited-state can be manipulated through mutation, independent of perturbations of the ground-state structures.
Title: Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins.
Results show that the flexible subdomains of adk fold into their native structure in a noncooperative manner with respect to the CORE subdomain.
Title: Noncooperative folding of subdomains in adenylate kinase.
Results describe the atomistic mechanism of conformational transition in adenylate kinase.
Title: The atomistic mechanism of conformational transition in adenylate kinase: a TEE-REX molecular dynamics study.
N-terminus verified by Edman degradation on complete protein
Title: Protein identification with N and C-terminal sequence tags in proteome projects.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables AMP binding	IDA Inferred from Direct Assay more info	PubMed
enables ATP binding	IDA Inferred from Direct Assay more info	PubMed
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables adenylate kinase activity	IBA Inferred from Biological aspect of Ancestor more info
enables adenylate kinase activity	IDA Inferred from Direct Assay more info	PubMed
enables adenylate kinase activity	IEA Inferred from Electronic Annotation more info
enables adenylate kinase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables kinase activity	IEA Inferred from Electronic Annotation more info
enables magnesium ion binding	IDA Inferred from Direct Assay more info	PubMed
enables nucleobase-containing compound kinase activity	IEA Inferred from Electronic Annotation more info
enables nucleoside diphosphate kinase activity	IBA Inferred from Biological aspect of Ancestor more info
enables nucleoside diphosphate kinase activity	IDA Inferred from Direct Assay more info	PubMed
enables nucleoside monophosphate kinase activity	IEA Inferred from Electronic Annotation more info
enables nucleotide binding	IEA Inferred from Electronic Annotation more info
enables phosphotransferase activity, phosphate group as acceptor	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	TAS Traceable Author Statement more info	PubMed
enables transferase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
acts_upstream_of_or_within ADP biosynthetic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in AMP salvage	IEA Inferred from Electronic Annotation more info
involved_in nucleobase-containing compound metabolic process	IEA Inferred from Electronic Annotation more info
involved_in nucleoside diphosphate metabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in nucleoside monophosphate metabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in nucleoside monophosphate phosphorylation	IEA Inferred from Electronic Annotation more info
involved_in nucleotide biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in organonitrogen compound biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in phosphorylation	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within purine ribonucleotide interconversion	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: adenylate kinase

NP_415007.1

EC 2.7.4.3

EC 2.7.4.4

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_000913.3 Reference assembly

Range

497175..497819

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NP_415007.1 adenylate kinase [Escherichia coli str. K-12 substr. MG1655]

See identical proteins and their annotated locations for NP_415007.1

Status: PROVISIONAL

UniProtKB/TrEMBL

A0AA88EQI2

Conserved Domains (1) summary

PRK00279
Location:1 → 214

adk; adenylate kinase; Reviewed