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UniProtKB - P16304 (KAD_BACSU)
Protein
Adenylate kinase
Gene
adk
Organism
Bacillus subtilis (strain 168)
Status
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 annotationCatalytic activityi
- EC:2.7.4.3UniRule annotation
Temperature dependencei
Optimum temperature is 45 degrees Celsius. Thermal denaturation midpoint (Tm) is 47.6 degrees Celsius and is raised to 66.0 degrees Celsius when AK is complexed with the inhibitor Ap5A.1 Publication
: AMP biosynthesis via salvage pathway Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes AMP from ADP.UniRule annotation 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 31 | AMPUniRule annotation2 Publications | 1 | |
Binding sitei | 36 | AMPUniRule annotation2 Publications | 1 | |
Binding sitei | 92 | AMPUniRule annotation2 Publications | 1 | |
Binding sitei | 127 | ATPUniRule annotation2 Publications | 1 | |
Metal bindingi | 130 | Zinc; structuralUniRule annotation2 Publications | 1 | |
Metal bindingi | 133 | Zinc; structuralUniRule annotation2 Publications | 1 | |
Metal bindingi | 150 | Zinc; structuralUniRule annotation2 Publications | 1 | |
Metal bindingi | 153 | Zinc; structuralUniRule annotation2 Publications | 1 | |
Binding sitei | 160 | AMPUniRule annotation2 Publications | 1 | |
Binding sitei | 171 | AMPUniRule annotation2 Publications | 1 | |
Binding sitei | 199 | ATP; via carbonyl oxygenUniRule annotation2 Publications | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 10 – 15 | ATPUniRule annotation2 Publications | 6 | |
Nucleotide bindingi | 57 – 59 | AMPUniRule annotation2 Publications | 3 | |
Nucleotide bindingi | 85 – 88 | AMPUniRule annotation2 Publications | 4 | |
Nucleotide bindingi | 136 – 137 | ATPUniRule annotation2 Publications | 2 |
GO - Molecular functioni
- adenylate kinase activity Source: GO_Central
- ATP binding Source: UniProtKB-UniRule
- nucleoside diphosphate kinase activity Source: GO_Central
- zinc ion binding Source: UniProtKB-UniRule
GO - Biological processi
- AMP salvage Source: UniProtKB-UniPathway
- nucleoside diphosphate metabolic process Source: GO_Central
- nucleoside monophosphate metabolic process Source: GO_Central
Keywordsi
Molecular function | Kinase, Transferase |
Biological process | Nucleotide biosynthesis |
Ligand | ATP-binding, Metal-binding, Nucleotide-binding, Zinc |
Enzyme and pathway databases
BioCyci | BSUB:BSU01370-MONOMER |
BRENDAi | 2.7.4.3, 658 |
SABIO-RKi | P16304 |
UniPathwayi | UPA00588;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 Superoxide-inducible protein 16 Short name: SOI16 |
Gene namesi | Name:adkUniRule annotation Ordered Locus Names:BSU01370 |
Organismi | Bacillus subtilis (strain 168) |
Taxonomic identifieri | 224308 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000158730 | 1 – 217 | Adenylate kinaseAdd BLAST | 217 |
Proteomic databases
jPOSTi | P16304 |
PaxDbi | P16304 |
PRIDEi | P16304 |
Expressioni
Inductioni
By superoxide.
Interactioni
Subunit structurei
Monomer.
UniRule annotation1 PublicationProtein-protein interaction databases
IntActi | P16304, 1 interactor |
MINTi | P16304 |
STRINGi | 224308.BSU01370 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
AlphaFoldDBi | P16304 |
SMRi | P16304 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P16304 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 30 – 59 | NMPUniRule annotation2 PublicationsAdd BLAST | 30 | |
Regioni | 126 – 163 | LIDUniRule annotation2 PublicationsAdd BLAST | 38 |
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 annotation3 Publications
Sequence similaritiesi
Belongs to the adenylate kinase family.UniRule annotation
Phylogenomic databases
eggNOGi | COG0563, Bacteria |
InParanoidi | P16304 |
OMAi | FHNRMRV |
PhylomeDBi | P16304 |
Family and domain databases
CDDi | cd01428, ADK, 1 hit |
Gene3Di | 3.40.50.300, 1 hit |
HAMAPi | MF_00235, Adenylate_kinase_Adk, 1 hit |
InterProi | View protein in InterPro IPR006259, Adenyl_kin_sub IPR000850, Adenylat/UMP-CMP_kin IPR033690, Adenylat_kinase_CS IPR007862, Adenylate_kinase_lid-dom IPR027417, P-loop_NTPase |
PANTHERi | PTHR23359, PTHR23359, 1 hit |
Pfami | View protein in Pfam PF05191, ADK_lid, 1 hit |
PRINTSi | PR00094, ADENYLTKNASE |
SUPFAMi | SSF52540, SSF52540, 1 hit |
TIGRFAMsi | TIGR01351, adk, 1 hit |
PROSITEi | View protein in PROSITE PS00113, ADENYLATE_KINASE, 1 hit |
i Sequence
Sequence statusi: Complete.
P16304-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MNLVLMGLPG AGKGTQGERI VEDYGIPHIS TGDMFRAAMK EETPLGLEAK
60 70 80 90 100
SYIDKGELVP DEVTIGIVKE RLGKDDCERG FLLDGFPRTV AQAEALEEIL
110 120 130 140 150
EEYGKPIDYV INIEVDKDVL MERLTGRRIC SVCGTTYHLV FNPPKTPGIC
160 170 180 190 200
DKDGGELYQR ADDNEETVSK RLEVNMKQTQ PLLDFYSEKG YLANVNGQQD
210
IQDVYADVKD LLGGLKK
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D00619 Genomic DNA Translation: BAA00496.1 L47971 Genomic DNA Translation: AAB06820.1 AL009126 Genomic DNA Translation: CAB11913.1 M31102 Genomic DNA Translation: AAB59119.1 X51329 Genomic DNA Translation: CAA35713.1 |
PIRi | JS0492 |
RefSeqi | NP_388018.1, NC_000964.3 WP_004399686.1, NZ_JNCM01000029.1 |
Genome annotation databases
EnsemblBacteriai | CAB11913; CAB11913; BSU_01370 |
GeneIDi | 938508 |
KEGGi | bsu:BSU01370 |
PATRICi | fig|224308.179.peg.140 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D00619 Genomic DNA Translation: BAA00496.1 L47971 Genomic DNA Translation: AAB06820.1 AL009126 Genomic DNA Translation: CAB11913.1 M31102 Genomic DNA Translation: AAB59119.1 X51329 Genomic DNA Translation: CAA35713.1 |
PIRi | JS0492 |
RefSeqi | NP_388018.1, NC_000964.3 WP_004399686.1, NZ_JNCM01000029.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1P3J | X-ray | 1.90 | A | 1-217 | [»] | |
2EU8 | X-ray | 1.80 | A/B | 1-216 | [»] | |
2OO7 | X-ray | 1.80 | A/B | 1-217 | [»] | |
2ORI | X-ray | 1.80 | A/B | 1-216 | [»] | |
2OSB | X-ray | 1.80 | A/B | 1-216 | [»] | |
2P3S | X-ray | 1.80 | A | 1-217 | [»] | |
2QAJ | X-ray | 1.80 | A/B | 1-217 | [»] | |
3DKV | X-ray | 1.82 | A | 1-217 | [»] | |
3DL0 | X-ray | 1.58 | A/B | 1-216 | [»] | |
4MKF | X-ray | 1.70 | A/B | 1-217 | [»] | |
4MKG | X-ray | 1.45 | A | 1-217 | [»] | |
4MKH | X-ray | 1.50 | A | 1-212 | [»] | |
4QBF | X-ray | 1.80 | A | 1-217 | [»] | |
4QBG | X-ray | 1.37 | B | 1-217 | [»] | |
4TYP | X-ray | 2.90 | A/B/C/D | 1-217 | [»] | |
4TYQ | X-ray | 1.65 | A/B | 1-217 | [»] | |
5X6I | X-ray | 2.00 | A | 1-217 | [»] | |
AlphaFoldDBi | P16304 | |||||
SMRi | P16304 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
IntActi | P16304, 1 interactor |
MINTi | P16304 |
STRINGi | 224308.BSU01370 |
Chemistry databases
DrugBanki | DB01717, Bis(Adenosine)-5'-Pentaphosphate |
Proteomic databases
jPOSTi | P16304 |
PaxDbi | P16304 |
PRIDEi | P16304 |
Genome annotation databases
EnsemblBacteriai | CAB11913; CAB11913; BSU_01370 |
GeneIDi | 938508 |
KEGGi | bsu:BSU01370 |
PATRICi | fig|224308.179.peg.140 |
Phylogenomic databases
eggNOGi | COG0563, Bacteria |
InParanoidi | P16304 |
OMAi | FHNRMRV |
PhylomeDBi | P16304 |
Enzyme and pathway databases
UniPathwayi | UPA00588;UER00649 |
BioCyci | BSUB:BSU01370-MONOMER |
BRENDAi | 2.7.4.3, 658 |
SABIO-RKi | P16304 |
Miscellaneous databases
EvolutionaryTracei | P16304 |
Family and domain databases
CDDi | cd01428, ADK, 1 hit |
Gene3Di | 3.40.50.300, 1 hit |
HAMAPi | MF_00235, Adenylate_kinase_Adk, 1 hit |
InterProi | View protein in InterPro IPR006259, Adenyl_kin_sub IPR000850, Adenylat/UMP-CMP_kin IPR033690, Adenylat_kinase_CS IPR007862, Adenylate_kinase_lid-dom IPR027417, P-loop_NTPase |
PANTHERi | PTHR23359, PTHR23359, 1 hit |
Pfami | View protein in Pfam PF05191, ADK_lid, 1 hit |
PRINTSi | PR00094, ADENYLTKNASE |
SUPFAMi | SSF52540, SSF52540, 1 hit |
TIGRFAMsi | TIGR01351, adk, 1 hit |
PROSITEi | View protein in PROSITE PS00113, ADENYLATE_KINASE, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | KAD_BACSU | |
Accessioni | P16304Primary (citable) accession number: P16304 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1990 |
Last sequence update: | February 1, 1991 | |
Last modified: | May 25, 2022 | |
This is version 173 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families