Skip Header

Contribute Send feedback
Read comments (?) or add your own

P27142 (KAD_GEOSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 18, 2012. Version 85. 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
Gene names
Name:adk
OrganismGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeGeobacillus

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. This small ubiquitous enzyme involved in the energy metabolism and nucleotide synthesis, is essential for maintenance and cell growth. HAMAP MF_00235

Catalytic activity

ATP + AMP = 2 ADP. HAMAP MF_00235

Pathway

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

Subunit structure

Monomer.

Subcellular location

Cytoplasm HAMAP MF_00235.

Domain

Consists of three domains, a large central CORE domain and two small peripheral domains, AMP binding and LID. The LID domain closes over the site of phosphoryl transfer upon ATP binding. HAMAP MF_00235

Miscellaneous

The zinc ion does not participate in catalysis. It has a structural role in stabilizing the LID domain, which does not seem to be involved in directly binding DNA/RNA. HAMAP 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 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 processnucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

adenylate kinase activity

Inferred from electronic annotation. Source: EC

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 MF_00235
PRO_0000158729

Regions

Nucleotide binding7 – 159ATP HAMAP MF_00235
Nucleotide binding31 – 5929AMP HAMAP MF_00235
Region128 – 15932LID HAMAP MF_00235

Sites

Metal binding1301Zinc
Metal binding1331Zinc
Metal binding1501Zinc
Metal binding1531Zinc

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: 1554691] [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: 9715904] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF COMPLEX WITH THE INHIBITOR AP5A.

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...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_00235. Adenylate_kinase_Adk.
[Tree]
InterProIPR006259. Adenyl_kin_sub.
IPR000850. Adenylate_kin.
IPR007862. Adenylate_kinase_lid-dom.
[Graphical view]
PANTHERPTHR23359. Adenylate_kin. 1 hit.
PfamPF00406. ADK. 1 hit.
PF05191. ADK_lid. 1 hit.
[Graphical view]
PRINTSPR00094. ADENYLTKNASE.
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 18, 2012
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families