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Q92GY7 (KAD_RICCN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adenylate kinase

Short name=AK
EC=2.7.4.3
Alternative name(s):
ATP-AMP transphosphorylase
ATP:AMP phosphotransferase
Adenylate monophosphate kinase
Gene names
Name:adk
Ordered Locus Names:RC0985
OrganismRickettsia conorii (strain ATCC VR-613 / Malish 7) [Complete proteome] [HAMAP]
Taxonomic identifier272944 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length212 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_00235

Catalytic activity

ATP + AMP = 2 ADP. HAMAP-Rule MF_00235

Pathway

Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. HAMAP-Rule MF_00235

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00235

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00235.

Domain

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 By similarity. HAMAP-Rule MF_00235

Sequence similarities

Belongs to the adenylate kinase family.

Ontologies

Keywords
   Biological processNucleotide biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processAMP salvage

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

adenylate kinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 212212Adenylate kinase HAMAP-Rule MF_00235
PRO_0000158838

Regions

Nucleotide binding10 – 156ATP By similarity
Nucleotide binding57 – 593AMP By similarity
Nucleotide binding85 – 884AMP By similarity
Nucleotide binding132 – 1332ATP By similarity
Region30 – 5930NMPbind By similarity
Region122 – 16039LID By similarity

Sites

Metal binding1261Zinc; structural By similarity
Metal binding1291Zinc; structural By similarity
Metal binding1461Zinc; structural By similarity
Metal binding1491Zinc; structural By similarity
Binding site361AMP By similarity
Binding site921AMP By similarity
Binding site1231ATP By similarity
Binding site1571AMP By similarity
Binding site1681AMP By similarity
Binding site1961ATP; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92GY7 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: BF785765826527A4

FASTA21224,497
        10         20         30         40         50         60 
MMVIFLGPPG AGKGTQGKKI AKKIDLPHIA IGDIFRTIIK TSTSEAELIN NYVKQGELIP 

        70         80         90        100        110        120 
NEIVNQVIKN FLLSSEYKNG YILDGYPRNL EQAKFFESFI KEKIKIIYFD VSDELLIKRI 

       130        140        150        160        170        180 
LGRYSCKNCG KIYNRYFVQP KTDNVCDVCG SSTFDYRKDD NEEVIKKRIE VYKTETYPLI 

       190        200        210 
DYYKNSGNFY IVNGSKNEQE IEIDIQKILK IN 

« Hide

References

[1]"Mechanisms of evolution in Rickettsia conorii and R. prowazekii."
Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.
Science 293:2093-2098(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006914 Genomic DNA. Translation: AAL03523.1.
PIRA97823.
RefSeqNP_360622.1. NC_003103.1.

3D structure databases

ProteinModelPortalQ92GY7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272944.RC0985.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL03523; AAL03523; RC0985.
GeneID928128.
KEGGrco:RC0985.
PATRIC17889376. VBIRicCon45613_1125.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0563.
HOGENOMHOG000238772.
KOK00939.
OMAQKIMESG.
OrthoDBEOG679TH4.
ProtClustDBPRK00279.

Enzyme and pathway databases

UniPathwayUPA00588; UER00649.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_00235. Adenylate_kinase_Adk.
InterProIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR23359. PTHR23359. 1 hit.
PfamPF05191. ADK_lid. 1 hit.
[Graphical view]
PRINTSPR00094. ADENYLTKNASE.
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR01351. adk. 1 hit.
PROSITEPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKAD_RICCN
AccessionPrimary (citable) accession number: Q92GY7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Rickettsia conorii

(strain Malish 7): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways