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Protein

Adenylate kinase

Gene

adk

Organism
Rickettsia conorii (strain ATCC VR-613 / Malish 7)
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 sitei36AMPUniRule annotation1
Binding sitei92AMPUniRule annotation1
Binding sitei123ATPUniRule annotation1
Metal bindingi126Zinc; structuralUniRule annotation1
Metal bindingi129Zinc; structuralUniRule annotation1
Metal bindingi146Zinc; structuralUniRule annotation1
Metal bindingi149Zinc; structuralUniRule annotation1
Binding sitei157AMPUniRule annotation1
Binding sitei168AMPUniRule annotation1
Binding sitei196ATP; via carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 15ATPUniRule annotation6
Nucleotide bindingi57 – 59AMPUniRule annotation3
Nucleotide bindingi85 – 88AMPUniRule annotation4
Nucleotide bindingi132 – 133ATPUniRule 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

BioCyciRCON272944:G1FZG-1619-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:RC0985
OrganismiRickettsia conorii (strain ATCC VR-613 / Malish 7)
Taxonomic identifieri272944 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group
Proteomesi
  • UP000000816 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001588381 – 212Adenylate kinaseAdd BLAST212

Proteomic databases

PRIDEiQ92GY7

Interactioni

Subunit structurei

Monomer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ92GY7
SMRiQ92GY7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni30 – 59NMPbindUniRule annotationAdd BLAST30
Regioni122 – 160LIDUniRule annotationAdd BLAST39

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

HOGENOMiHOG000238772
KOiK00939
OMAiEKFTSQG
OrthoDBiPOG091H01SU

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.

Q92GY7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMVIFLGPPG AGKGTQGKKI AKKIDLPHIA IGDIFRTIIK TSTSEAELIN
60 70 80 90 100
NYVKQGELIP NEIVNQVIKN FLLSSEYKNG YILDGYPRNL EQAKFFESFI
110 120 130 140 150
KEKIKIIYFD VSDELLIKRI LGRYSCKNCG KIYNRYFVQP KTDNVCDVCG
160 170 180 190 200
SSTFDYRKDD NEEVIKKRIE VYKTETYPLI DYYKNSGNFY IVNGSKNEQE
210
IEIDIQKILK IN
Length:212
Mass (Da):24,497
Last modified:December 1, 2001 - v1
Checksum:iBF785765826527A4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006914 Genomic DNA Translation: AAL03523.1
PIRiA97823
RefSeqiWP_010977577.1, NC_003103.1

Genome annotation databases

EnsemblBacteriaiAAL03523; AAL03523; RC0985
GeneIDi928128
KEGGirco:RC0985
PATRICifig|272944.4.peg.1125

Similar proteinsi

Entry informationi

Entry nameiKAD_RICCN
AccessioniPrimary (citable) accession number: Q92GY7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: December 1, 2001
Last modified: May 23, 2018
This is version 100 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

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