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P27142 (KAD_GEOSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. 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
OrganismGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length217 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Subcellular location

Cytoplasm 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. HAMAP-Rule MF_00235

Sequence similarities

Belongs to the adenylate kinase family.

Biophysicochemical properties

Temperature dependence:

Optimum temperature is 55 degrees Celsius. Thermal denaturation midpoint (Tm) is 74.5 degrees Celsius. HAMAP-Rule MF_00235

Ontologies

Keywords
   Biological processNucleotide biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Transferase
   Technical term3D-structure
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

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 217217Adenylate kinase HAMAP-Rule MF_00235
PRO_0000158729

Regions

Nucleotide binding10 – 156ATP HAMAP-Rule MF_00235
Nucleotide binding57 – 593AMP HAMAP-Rule MF_00235
Nucleotide binding85 – 884AMP HAMAP-Rule MF_00235
Nucleotide binding136 – 1372ATP HAMAP-Rule MF_00235
Region30 – 5930NMPbind HAMAP-Rule MF_00235
Region126 – 16338LID HAMAP-Rule MF_00235

Sites

Metal binding1301Zinc; structural
Metal binding1331Zinc; structural
Metal binding1501Zinc; structural
Metal binding1531Zinc; structural
Binding site311AMP
Binding site361AMP
Binding site921AMP
Binding site1271ATP
Binding site1601AMP
Binding site1711AMP
Binding site1991ATP; via carbonyl oxygen

Secondary structure

.......................................... 217
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27142 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: D8701931117C53CF

FASTA21724,143
        10         20         30         40         50         60 
MNLVLMGLPG AGKGTQAEKI VAAYGIPHIS TGDMFRAAMK EGTPLGLQAK QYMDRGDLVP 

        70         80         90        100        110        120 
DEVTIGIVRE RLSKDDCQNG FLLDGFPRTV AQAEALETML ADIGRKLDYV IHIDVRQDVL 

       130        140        150        160        170        180 
MERLTGRRIC RNCGATYHLI FHPPAKPGVC DKCGGELYQR ADDNEATVAN RLEVNMKQMK 

       190        200        210 
PLVDFYEQKG YLRNINGEQD MEKVFADIRE LLGGLAR 

« Hide

References

[1]"Zinc, a novel structural element found in the family of bacterial adenylate kinases."
Glaser P., Presecan E., Delepierre M., Surewicz W.K., Mantsch H.H., Barzu O., Gilles A.M.
Biochemistry 31:3038-3043(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ZINC ION.
[2]Schiltz E., Buerkle S., Stiehle H., Mader B., Schulz G.E.
Submitted (APR-1992) to the PIR data bank
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Crystal structures of Bacillus stearothermophilus adenylate kinase with bound Ap5A, Mg2+ Ap5A, and Mn2+ Ap5A reveal an intermediate lid position and six coordinate octahedral geometry for bound Mg2+ and Mn2+."
Berry M.B., Phillips G.N. Jr.
Proteins 32:276-288(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF COMPLEX WITH BI-SUBSTRATE ANALOG AP5A AND ZINC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M88104 Genomic DNA. Translation: AAA22205.1.
PIRKIBSAF. B42196.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZINX-ray1.60A1-217[»]
1ZIOX-ray1.96A1-217[»]
1ZIPX-ray1.85A1-217[»]
ProteinModelPortalP27142.
SMRP27142. Positions 1-217.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP27142.
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...

Other

EvolutionaryTraceP27142.

Entry information

Entry nameKAD_GEOSE
AccessionPrimary (citable) accession number: P27142
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: April 16, 2014
This is version 96 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways