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Protein

Adenylate kinase

Gene

adk

Organism
Sporosarcina globispora (Bacillus globisporus)
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 annotation

Temperature dependencei

Optimum temperature is 35 degrees Celsius. Thermal denaturation midpoint (Tm) is 43.3 degrees Celsius and is raised to 60.4 degrees Celsius when AK is complexed with the inhibitor Ap5A.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)
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

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
OrganismiSporosarcina globispora (Bacillus globisporus)
Taxonomic identifieri1459 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPlanococcaceaeSporosarcina

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_00001587241 – 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
Beta strandi81 – 85Combined sources5
Helixi90 – 102Combined sources13
Beta strandi109 – 114Combined sources6
Helixi117 – 125Combined sources9
Beta strandi126 – 130Combined sources5
Turni131 – 133Combined sources3
Beta strandi136 – 138Combined sources3
Turni139 – 141Combined sources3
Turni151 – 153Combined sources3
Beta strandi156 – 158Combined sources3
Helixi165 – 187Combined sources23
Turni188 – 190Combined sources3
Beta strandi192 – 196Combined sources5
Helixi201 – 212Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1S3GX-ray2.25A1-217[»]
ProteinModelPortaliP84139.
SMRiP84139.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP84139.

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.

P84139-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNIVLMGLPG AGKGTQADRI VEKYGTPHIS TGDMFRAAIQ EGTELGVKAK
60 70 80 90 100
SFMDQGALVP DEVTIGIVRE RLSKSDCDNG FLLDGFPRTV PQAEALDQLL
110 120 130 140 150
ADMGRKIEHV LNIQVEKEEL IARLTGRRIC KVCGTSYHLL FNPPQVEGKC
160 170 180 190 200
DKDGGELYQR ADDNPDTVTN RLEVNMNQTA PLLAFYDSKE VLVNINGQKD
210
IKDVFKDLDV ILQGNGQ
Length:217
Mass (Da):23,888
Last modified:September 13, 2004 - v1
Checksum:iA8E28D5CF7C747AE
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1S3GX-ray2.25A1-217[»]
ProteinModelPortaliP84139.
SMRiP84139.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00588; UER00649.

Miscellaneous databases

EvolutionaryTraceiP84139.

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_SPOGL
AccessioniPrimary (citable) accession number: P84139
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: September 13, 2004
Last modified: November 30, 2016
This is version 72 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, Direct protein sequencing

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.