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Protein

Adenylate kinase

Gene

adk

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.UniRule annotation2 Publications

Catalytic activityi

ATP + AMP = 2 ADP.UniRule annotation1 Publication

Kineticsi

  1. KM=51 µM for ATP (at pH 7.4 and 30 degrees Celsius)1 Publication
  2. KM=38 µM for AMP (at pH 7.4 and 30 degrees Celsius)1 Publication
  3. KM=92 µM for ADP (at pH 7.4 and 30 degrees Celsius)1 Publication
  1. Vmax=1020 µmol/min/mg enzyme for the forward reaction (at pH 7.4 and 30 degrees Celsius)1 Publication
  2. Vmax=605 µmol/min/mg enzyme for the reverse reaction (at pH 7.4 and 30 degrees Celsius)1 Publication

Temperature dependencei

Optimum temperature is 45 degrees Celsius. Thermostable. Is half-inactivated at 52 degrees Celsius.1 Publication

Pathwayi: AMP biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes AMP from ADP.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Adenylate kinase (adk)
This subpathway is part of the pathway AMP biosynthesis via salvage pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from ADP, the pathway AMP biosynthesis via salvage pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei31AMPUniRule annotation5 Publications1
Binding sitei36AMPUniRule annotation5 Publications1
Binding sitei92AMPUniRule annotation5 Publications1
Binding sitei119ATP1 Publication1
Binding sitei123ATPUniRule annotation5 Publications1
Binding sitei156AMPUniRule annotation5 Publications1
Binding sitei167AMPUniRule annotation3 Publications1
Binding sitei200ATP; via carbonyl oxygenUniRule annotation5 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 15ATPUniRule annotation5 Publications6
Nucleotide bindingi57 – 59AMPUniRule annotation5 Publications3
Nucleotide bindingi85 – 88AMPUniRule annotation3 Publications4
Nucleotide bindingi132 – 133ATPUniRule annotation4 Publications2

GO - Molecular functioni

  • adenylate kinase activity Source: EcoCyc
  • AMP binding Source: EcoCyc
  • ATP binding Source: EcoCyc
  • magnesium ion binding Source: EcoCyc

GO - Biological processi

  • ADP biosynthetic process Source: EcoliWiki
  • AMP salvage Source: UniProtKB-UniPathway
  • phospholipid biosynthetic process Source: EcoliWiki
  • purine ribonucleotide interconversion Source: EcoCyc
  • RNA biosynthetic process Source: EcoliWiki
  • translation Source: EcoliWiki

Keywordsi

Molecular functionKinase, Transferase
Biological processNucleotide biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:ADENYL-KIN-MONOMER
MetaCyc:ADENYL-KIN-MONOMER
BRENDAi2.7.4.3 2026
SABIO-RKiP69441
UniPathwayiUPA00588; UER00649

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate kinaseUniRule annotation (EC:2.7.4.3UniRule annotation)
Short name:
AKUniRule annotation
Alternative name(s):
ATP-AMP transphosphorylaseUniRule annotation
ATP:AMP phosphotransferaseUniRule annotation
Adenylate monophosphate kinaseUniRule annotation
Gene namesi
Name:adkUniRule annotation
Synonyms:dnaW, plsA
Ordered Locus Names:b0474, JW0463
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10032 adk

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • cytosol Source: EcoCyc

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi9P → G: No loss of enzyme activity. 2 Publications1
Mutagenesisi10G → V: No loss of enzyme activity. 3 Publications1
Mutagenesisi13K → Q: Drastic reduction in enzyme activity. 2 Publications1

Chemistry databases

DrugBankiDB01717 Bis(Adenosine)-5'-Pentaphosphate

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001587671 – 214Adenylate kinaseAdd BLAST214

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei192N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP69441
PaxDbiP69441
PRIDEiP69441

2D gel databases

SWISS-2DPAGEiP69441

PTM databases

iPTMnetiP69441

Interactioni

Subunit structurei

Monomer.UniRule annotation3 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi4261613, 20 interactors
DIPiDIP-47903N
IntActiP69441, 13 interactors
STRINGi316385.ECDH10B_0430

Structurei

Secondary structure

1214
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 8Combined sources7
Helixi13 – 24Combined sources12
Beta strandi28 – 30Combined sources3
Helixi31 – 41Combined sources11
Turni44 – 46Combined sources3
Helixi47 – 49Combined sources3
Helixi50 – 55Combined sources6
Helixi61 – 72Combined sources12
Helixi75 – 77Combined sources3
Beta strandi81 – 85Combined sources5
Helixi90 – 99Combined sources10
Beta strandi104 – 110Combined sources7
Helixi113 – 115Combined sources3
Helixi116 – 120Combined sources5
Beta strandi123 – 125Combined sources3
Turni127 – 129Combined sources3
Beta strandi132 – 134Combined sources3
Turni135 – 137Combined sources3
Turni147 – 149Combined sources3
Helixi157 – 159Combined sources3
Helixi161 – 174Combined sources14
Turni175 – 177Combined sources3
Helixi178 – 187Combined sources10
Beta strandi190 – 197Combined sources8
Helixi202 – 213Combined sources12

3D structure databases

ProteinModelPortaliP69441
SMRiP69441
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP69441

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni30 – 59NMPbindUniRule annotation1 PublicationAdd BLAST30
Regioni122 – 159LIDUniRule annotation1 PublicationAdd BLAST38

Domaini

Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.UniRule annotation1 Publication

Sequence similaritiesi

Belongs to the adenylate kinase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CC8 Bacteria
COG0563 LUCA
HOGENOMiHOG000238772
InParanoidiP69441
KOiK00939
OMAiEKFTSQG
PhylomeDBiP69441

Family and domain databases

CDDicd01428 ADK, 1 hit
HAMAPiMF_00235 Adenylate_kinase_Adk, 1 hit
InterProiView protein in InterPro
IPR006259 Adenyl_kin_sub
IPR000850 Adenylat/UMP-CMP_kin
IPR033690 Adenylat_kinase_CS
IPR007862 Adenylate_kinase_lid-dom
IPR027417 P-loop_NTPase
PANTHERiPTHR23359 PTHR23359, 1 hit
PfamiView protein in Pfam
PF05191 ADK_lid, 1 hit
PRINTSiPR00094 ADENYLTKNASE
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR01351 adk, 1 hit
PROSITEiView protein in PROSITE
PS00113 ADENYLATE_KINASE, 1 hit

Sequencei

Sequence statusi: Complete.

P69441-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRIILLGAPG AGKGTQAQFI MEKYGIPQIS TGDMLRAAVK SGSELGKQAK
60 70 80 90 100
DIMDAGKLVT DELVIALVKE RIAQEDCRNG FLLDGFPRTI PQADAMKEAG
110 120 130 140 150
INVDYVLEFD VPDELIVDRI VGRRVHAPSG RVYHVKFNPP KVEGKDDVTG
160 170 180 190 200
EELTTRKDDQ EETVRKRLVE YHQMTAPLIG YYSKEAEAGN TKYAKVDGTK
210
PVAEVRADLE KILG
Length:214
Mass (Da):23,586
Last modified:August 13, 1987 - v1
Checksum:iBB917C84000A80EE
GO

Sequence cautioni

The sequence AAB40228 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03038 Genomic DNA Translation: CAA26840.1
U82664 Genomic DNA Translation: AAB40228.1 Different initiation.
U00096 Genomic DNA Translation: AAC73576.1
AP009048 Genomic DNA Translation: BAE76253.1
M38777 Genomic DNA Translation: AAA23461.1
D90259 Genomic DNA Translation: BAA14303.1
PIRiA24275 KIECA
RefSeqiNP_415007.1, NC_000913.3
WP_001220233.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73576; AAC73576; b0474
BAE76253; BAE76253; BAE76253
GeneIDi945097
KEGGiecj:JW0463
eco:b0474
PATRICifig|1411691.4.peg.1802

Similar proteinsi

Entry informationi

Entry nameiKAD_ECOLI
AccessioniPrimary (citable) accession number: P69441
Secondary accession number(s): P05082, P77123, Q2MBV3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: March 28, 2018
This is version 129 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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