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Protein

Adenylate kinase

Gene

adk

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Temperature dependencei

Optimum temperature is 55 degrees Celsius. Thermal denaturation midpoint (Tm) is 74.5 degrees Celsius.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei31 – 311AMP
Binding sitei36 – 361AMP
Binding sitei92 – 921AMP
Binding sitei127 – 1271ATP
Metal bindingi130 – 1301Zinc; structural
Metal bindingi133 – 1331Zinc; structural
Metal bindingi150 – 1501Zinc; structural
Metal bindingi153 – 1531Zinc; structural
Binding sitei160 – 1601AMP
Binding sitei171 – 1711AMP
Binding sitei199 – 1991ATP; via carbonyl oxygen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 156ATP
Nucleotide bindingi57 – 593AMP
Nucleotide bindingi85 – 884AMP
Nucleotide bindingi136 – 1372ATP

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

SABIO-RKP27142.
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
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 217217Adenylate kinasePRO_0000158729Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
217
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi13 – 2412Combined sources
Beta strandi28 – 303Combined sources
Helixi31 – 4111Combined sources
Helixi44 – 5512Combined sources
Helixi61 – 7212Combined sources
Helixi75 – 773Combined sources
Beta strandi81 – 855Combined sources
Helixi90 – 10213Combined sources
Beta strandi109 – 1146Combined sources
Helixi117 – 1259Combined sources
Beta strandi127 – 1304Combined sources
Turni131 – 1333Combined sources
Beta strandi136 – 1383Combined sources
Turni139 – 1413Combined sources
Turni151 – 1533Combined sources
Beta strandi156 – 1583Combined sources
Helixi161 – 1633Combined sources
Helixi165 – 17915Combined sources
Helixi181 – 1888Combined sources
Beta strandi192 – 1965Combined sources
Helixi201 – 21616Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZINX-ray1.60A1-217[»]
1ZIOX-ray1.96A1-217[»]
1ZIPX-ray1.85A1-217[»]
4QBHX-ray1.67A/B1-215[»]
4QBIX-ray1.67A/B1-215[»]
ProteinModelPortaliP27142.
SMRiP27142. Positions 1-217.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27142.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 5930NMPbindAdd
BLAST
Regioni126 – 16338LIDAdd
BLAST

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.

Sequence similaritiesi

Belongs to the adenylate kinase family.UniRule annotation

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PfamiPF05191. ADK_lid. 1 hit.
[Graphical view]
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01351. adk. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P27142-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLVLMGLPG AGKGTQAEKI VAAYGIPHIS TGDMFRAAMK EGTPLGLQAK
60 70 80 90 100
QYMDRGDLVP DEVTIGIVRE RLSKDDCQNG FLLDGFPRTV AQAEALETML
110 120 130 140 150
ADIGRKLDYV IHIDVRQDVL MERLTGRRIC RNCGATYHLI FHPPAKPGVC
160 170 180 190 200
DKCGGELYQR ADDNEATVAN RLEVNMKQMK PLVDFYEQKG YLRNINGEQD
210
MEKVFADIRE LLGGLAR
Length:217
Mass (Da):24,143
Last modified:August 1, 1992 - v1
Checksum:iD8701931117C53CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88104 Genomic DNA. Translation: AAA22205.1.
PIRiB42196. KIBSAF.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88104 Genomic DNA. Translation: AAA22205.1.
PIRiB42196. KIBSAF.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZINX-ray1.60A1-217[»]
1ZIOX-ray1.96A1-217[»]
1ZIPX-ray1.85A1-217[»]
4QBHX-ray1.67A/B1-215[»]
4QBIX-ray1.67A/B1-215[»]
ProteinModelPortaliP27142.
SMRiP27142. Positions 1-217.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00588; UER00649.
SABIO-RKP27142.

Miscellaneous databases

EvolutionaryTraceiP27142.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PfamiPF05191. ADK_lid. 1 hit.
[Graphical view]
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01351. adk. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiKAD_GEOSE
AccessioniPrimary (citable) accession number: P27142
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: January 7, 2015
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.