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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 annotation1 Publication

Catalytic activityi

ATP + AMP = 2 ADP.UniRule annotation1 Publication

Temperature dependencei

Optimum temperature is 65 degrees Celsius. Thermal denaturation midpoint (Tm) is 74.5 degrees Celsius.1 Publication

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), Adenylate kinase (adk), Adenylate kinase (adk), 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 sitei31AMPUniRule annotation1 Publication1
Binding sitei36AMPUniRule annotation1 Publication1
Binding sitei92AMPUniRule annotation1 Publication1
Binding sitei127ATPUniRule annotation1 Publication1
Metal bindingi130Zinc; structuralUniRule annotation1 Publication1
Metal bindingi133Zinc; structuralUniRule annotation1 Publication1
Metal bindingi150Zinc; structuralUniRule annotation1 Publication1
Metal bindingi153Zinc; structuralUniRule annotation1 Publication1
Binding sitei160AMPUniRule annotation1 Publication1
Binding sitei171AMPUniRule annotation1 Publication1
Binding sitei199ATP; via carbonyl oxygenUniRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 15ATPUniRule annotation1 Publication6
Nucleotide bindingi57 – 59AMPUniRule annotation1 Publication3
Nucleotide bindingi85 – 88AMPUniRule annotation1 Publication4
Nucleotide bindingi136 – 137ATPUniRule annotation1 Publication2

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 annotation1 Publication)
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

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001587291 – 217Adenylate kinaseAdd BLAST217

Interactioni

Subunit structurei

Monomer.UniRule annotation

Structurei

Secondary structure

1217
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Helixi13 – 24Combined sources12
Beta strandi28 – 30Combined sources3
Helixi31 – 41Combined sources11
Helixi44 – 55Combined sources12
Helixi61 – 72Combined sources12
Helixi75 – 77Combined sources3
Beta strandi81 – 85Combined sources5
Helixi90 – 102Combined sources13
Beta strandi109 – 114Combined sources6
Helixi117 – 125Combined sources9
Beta strandi127 – 130Combined sources4
Turni131 – 133Combined sources3
Beta strandi136 – 138Combined sources3
Turni139 – 141Combined sources3
Turni151 – 153Combined sources3
Beta strandi156 – 158Combined sources3
Helixi161 – 163Combined sources3
Helixi165 – 179Combined sources15
Helixi181 – 188Combined sources8
Beta strandi192 – 196Combined sources5
Helixi201 – 216Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27142.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni30 – 59NMPbindUniRule annotation1 PublicationAdd BLAST30
Regioni126 – 163LIDUniRule annotation1 PublicationAdd BLAST38

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 annotation2 Publications

Sequence similaritiesi

Belongs to the adenylate kinase family.UniRule annotation

Family and domain databases

CDDicd01428. ADK. 1 hit.
Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk. 1 hit.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR033690. Adenylat_kinase_CS.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00588; UER00649.
SABIO-RKP27142.

Miscellaneous databases

EvolutionaryTraceiP27142.

Family and domain databases

CDDicd01428. ADK. 1 hit.
Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk. 1 hit.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR033690. Adenylat_kinase_CS.
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...

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: November 30, 2016
This is version 109 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

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 one 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.