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Protein

Adenylate kinase

Gene

adk

Organism
Mycoplasma pneumoniae (strain ATCC 29342 / M129)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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 annotation

Catalytic activityi

ATP + AMP = 2 ADP.UniRule annotation

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 sitei35AMPUniRule annotation1
Binding sitei40AMPUniRule annotation1
Binding sitei98AMPUniRule annotation1
Binding sitei129ATPUniRule annotation1
Metal bindingi132Zinc; structuralUniRule annotation1
Metal bindingi135Zinc; structuralUniRule annotation1
Metal bindingi152Zinc; structuralUniRule annotation1
Metal bindingi155Zinc; structuralUniRule annotation1
Binding sitei162AMPUniRule annotation1
Binding sitei173AMPUniRule annotation1
Binding sitei211ATP; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi14 – 19ATPUniRule annotation6
Nucleotide bindingi61 – 63AMPUniRule annotation3
Nucleotide bindingi91 – 94AMPUniRule annotation4
Nucleotide bindingi138 – 139ATPUniRule annotation2

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BioCyciMPNE272634:G1GJ3-298-MONOMER
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
Ordered Locus Names:MPN_185
ORF Names:MP646
OrganismiMycoplasma pneumoniae (strain ATCC 29342 / M129)
Taxonomic identifieri272634 [NCBI]
Taxonomic lineageiBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma
Proteomesi
  • UP000000808 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001588041 – 215Adenylate kinaseAdd BLAST215

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

IntActiQ50299, 1 interactor

Structurei

3D structure databases

ProteinModelPortaliQ50299
SMRiQ50299
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni34 – 63NMPbindUniRule annotationAdd BLAST30
Regioni128 – 165LIDUniRule annotationAdd 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. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.UniRule annotation

Sequence similaritiesi

Belongs to the adenylate kinase family.UniRule annotation

Phylogenomic databases

KOiK00939
OMAiVKNRWIH

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
IPR036193 ADK_active_lid_dom_sf
IPR027417 P-loop_NTPase
PANTHERiPTHR23359 PTHR23359, 1 hit
PfamiView protein in Pfam
PF05191 ADK_lid, 1 hit
PRINTSiPR00094 ADENYLTKNASE
SUPFAMiSSF52540 SSF52540, 2 hits
SSF57774 SSF57774, 1 hit
TIGRFAMsiTIGR01351 adk, 1 hit
PROSITEiView protein in PROSITE
PS00113 ADENYLATE_KINASE, 1 hit

Sequencei

Sequence statusi: Complete.

Q50299-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVMENKFLFL GAPGVGKGTL AKQVANTTGL FHLSTGDIFR SVMQEQGALS
60 70 80 90 100
QTLAHYMNQG LYVPDELTNQ TFWHFVTTHQ NELHKGFILD GYPRTLNQLE
110 120 130 140 150
FLQSKLQLDQ VFHLKLSDPQ VLVARILNRL VCPSCGSVYN KQSKPPLKAN
160 170 180 190 200
QCDRCHATLQ ARNDDTEAVI LKRLTLYEDT VKPLIEAFTK QGILTVIEAQ
210
LPLEQQVNLV QQLVH
Length:215
Mass (Da):24,255
Last modified:November 1, 1997 - v1
Checksum:i3F4258BEFA24E8E8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34795 Genomic DNA Translation: AAC43696.1
U00089 Genomic DNA Translation: AAB96294.1
PIRiS62823
RefSeqiNP_109873.1, NC_000912.1
WP_010874542.1, NC_000912.1

Genome annotation databases

EnsemblBacteriaiAAB96294; AAB96294; MPN_185
GeneIDi876756
KEGGimpn:MPN185
PATRICifig|272634.6.peg.203

Similar proteinsi

Entry informationi

Entry nameiKAD_MYCPN
AccessioniPrimary (citable) accession number: Q50299
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: March 28, 2018
This is version 115 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

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health