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Protein

Adenylate kinase

Gene

adk

Organism
Aquifex aeolicus (strain VF5)
Status
Reviewed-Annotation score: Annotation score: 4 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

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)
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 sitei89AMPUniRule annotation1 Publication1
Binding sitei120ATPUniRule annotation1 Publication1
Binding sitei124ATPUniRule annotation1 Publication1
Binding sitei161AMPUniRule annotation1 Publication1
Binding sitei189ATP; via carbonyl oxygenUniRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 15ATPUniRule annotation1 Publication6
Nucleotide bindingi57 – 59AMPUniRule annotation1 Publication3
Nucleotide bindingi82 – 85AMPUniRule annotation1 Publication4
Nucleotide bindingi133 – 134ATPUniRule 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, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.4.3. 396.
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
Ordered Locus Names:aq_078
OrganismiAquifex aeolicus (strain VF5)
Taxonomic identifieri224324 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
Proteomesi
  • UP000000798 Componenti: Chromosome

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_00001587181 – 206Adenylate kinaseAdd BLAST206

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi224324.aq_078.

Structurei

Secondary structure

1206
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Helixi13 – 24Combined sources12
Beta strandi27 – 30Combined sources4
Helixi31 – 41Combined sources11
Helixi44 – 55Combined sources12
Helixi61 – 71Combined sources11
Beta strandi74 – 76Combined sources3
Beta strandi78 – 82Combined sources5
Helixi87 – 99Combined sources13
Beta strandi106 – 111Combined sources6
Helixi114 – 122Combined sources9
Beta strandi124 – 126Combined sources3
Turni128 – 130Combined sources3
Beta strandi133 – 135Combined sources3
Turni136 – 138Combined sources3
Helixi151 – 153Combined sources3
Helixi155 – 168Combined sources14
Helixi171 – 177Combined sources7
Turni178 – 180Combined sources3
Beta strandi182 – 186Combined sources5
Helixi191 – 202Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RGXX-ray1.90A1-206[»]
2RH5X-ray2.48A/B/C1-206[»]
3SR0X-ray1.56A/B1-206[»]
4CF7X-ray1.59A/B1-206[»]
4IKEX-ray1.48A/B1-206[»]
4JKYX-ray2.37A/B1-203[»]
4JL5X-ray1.24A/B1-203[»]
4JL6X-ray1.65A/B1-203[»]
4JL8X-ray1.79A/B1-203[»]
4JLAX-ray2.12A/B1-203[»]
4JLBX-ray1.53A/B1-203[»]
4JLDX-ray1.55A/B1-203[»]
4JLOX-ray1.73A/B1-203[»]
4JLPX-ray1.43A/B1-203[»]
ProteinModelPortaliO66490.
SMRiO66490.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO66490.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni30 – 59NMPbindUniRule annotation1 PublicationAdd BLAST30
Regioni123 – 153LIDUniRule annotation1 PublicationAdd BLAST31

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.UniRule annotation1 Publication

Sequence similaritiesi

Belongs to the adenylate kinase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CC8. Bacteria.
COG0563. LUCA.
HOGENOMiHOG000238772.
InParanoidiO66490.
KOiK00939.
OMAiERIDAMG.
OrthoDBiPOG091H01SU.

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.
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF57774. SSF57774. 1 hit.
TIGRFAMsiTIGR01351. adk. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O66490-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MILVFLGPPG AGKGTQAKRL AKEKGFVHIS TGDILREAVQ KGTPLGKKAK
60 70 80 90 100
EYMERGELVP DDLIIALIEE VFPKHGNVIF DGFPRTVKQA EALDEMLEKK
110 120 130 140 150
GLKVDHVLLF EVPDEVVIER LSGRRINPET GEVYHVKYNP PPPGVKVIQR
160 170 180 190 200
EDDKPEVIKK RLEVYREQTA PLIEYYKKKG ILRIIDASKP VEEVYRQVLE

VIGDGN
Length:206
Mass (Da):23,231
Last modified:August 1, 1998 - v1
Checksum:i2310B49B11CBC71E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC06438.1.
PIRiG70307.
RefSeqiNP_213050.1. NC_000918.1.
WP_010879988.1. NC_000918.1.

Genome annotation databases

EnsemblBacteriaiAAC06438; AAC06438; aq_078.
GeneIDi1192503.
KEGGiaae:aq_078.
PATRICi20957855. VBIAquAeo85532_0068.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC06438.1.
PIRiG70307.
RefSeqiNP_213050.1. NC_000918.1.
WP_010879988.1. NC_000918.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RGXX-ray1.90A1-206[»]
2RH5X-ray2.48A/B/C1-206[»]
3SR0X-ray1.56A/B1-206[»]
4CF7X-ray1.59A/B1-206[»]
4IKEX-ray1.48A/B1-206[»]
4JKYX-ray2.37A/B1-203[»]
4JL5X-ray1.24A/B1-203[»]
4JL6X-ray1.65A/B1-203[»]
4JL8X-ray1.79A/B1-203[»]
4JLAX-ray2.12A/B1-203[»]
4JLBX-ray1.53A/B1-203[»]
4JLDX-ray1.55A/B1-203[»]
4JLOX-ray1.73A/B1-203[»]
4JLPX-ray1.43A/B1-203[»]
ProteinModelPortaliO66490.
SMRiO66490.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224324.aq_078.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC06438; AAC06438; aq_078.
GeneIDi1192503.
KEGGiaae:aq_078.
PATRICi20957855. VBIAquAeo85532_0068.

Phylogenomic databases

eggNOGiENOG4105CC8. Bacteria.
COG0563. LUCA.
HOGENOMiHOG000238772.
InParanoidiO66490.
KOiK00939.
OMAiERIDAMG.
OrthoDBiPOG091H01SU.

Enzyme and pathway databases

UniPathwayiUPA00588; UER00649.
BRENDAi2.7.4.3. 396.

Miscellaneous databases

EvolutionaryTraceiO66490.

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.
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF57774. SSF57774. 1 hit.
TIGRFAMsiTIGR01351. adk. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKAD_AQUAE
AccessioniPrimary (citable) accession number: O66490
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: November 30, 2016
This is version 113 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, Complete proteome, Reference proteome

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.