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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei31 – 311AMPUniRule annotation1 Publication
Binding sitei36 – 361AMPUniRule annotation1 Publication
Binding sitei92 – 921AMPUniRule annotation1 Publication
Binding sitei127 – 1271ATPUniRule annotation1 Publication
Metal bindingi130 – 1301Zinc; structuralUniRule annotation1 Publication
Metal bindingi133 – 1331Zinc; structuralUniRule annotation1 Publication
Metal bindingi150 – 1501Zinc; structuralUniRule annotation1 Publication
Metal bindingi153 – 1531Zinc; structuralUniRule annotation1 Publication
Binding sitei160 – 1601AMPUniRule annotation1 Publication
Binding sitei171 – 1711AMPUniRule annotation1 Publication
Binding sitei199 – 1991ATP; via carbonyl oxygenUniRule annotation1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 156ATPUniRule annotation1 Publication
Nucleotide bindingi57 – 593AMPUniRule annotation1 Publication
Nucleotide bindingi85 – 884AMPUniRule annotation1 Publication
Nucleotide bindingi136 – 1372ATPUniRule annotation1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 217217Adenylate kinasePRO_0000158724Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

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
Beta strandi81 – 855Combined sources
Helixi90 – 10213Combined sources
Beta strandi109 – 1146Combined sources
Helixi117 – 1259Combined sources
Beta strandi126 – 1305Combined sources
Turni131 – 1333Combined sources
Beta strandi136 – 1383Combined sources
Turni139 – 1413Combined sources
Turni151 – 1533Combined sources
Beta strandi156 – 1583Combined sources
Helixi165 – 18723Combined sources
Turni188 – 1903Combined sources
Beta strandi192 – 1965Combined sources
Helixi201 – 21212Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP84139.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 5930NMPbindUniRule annotation1 PublicationAdd
BLAST
Regioni126 – 16338LIDUniRule annotation1 PublicationAdd
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.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.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1S3GX-ray2.25A1-217[»]
ProteinModelPortaliP84139.
SMRiP84139. Positions 1-217.
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.
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: September 7, 2016
This is version 69 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.