Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Adenylate kinase

Gene

adk

Organism
Bacillus subtilis (strain 168)
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 annotation

Catalytic activityi

ATP + AMP = 2 ADP.UniRule 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

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 annotation2 Publications1
Binding sitei36AMPUniRule annotation2 Publications1
Binding sitei92AMPUniRule annotation2 Publications1
Binding sitei127ATPUniRule annotation2 Publications1
Metal bindingi130Zinc; structuralUniRule annotation2 Publications1
Metal bindingi133Zinc; structuralUniRule annotation2 Publications1
Metal bindingi150Zinc; structuralUniRule annotation2 Publications1
Metal bindingi153Zinc; structuralUniRule annotation2 Publications1
Binding sitei160AMPUniRule annotation2 Publications1
Binding sitei171AMPUniRule annotation2 Publications1
Binding sitei199ATP; via carbonyl oxygenUniRule annotation2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 15ATPUniRule annotation2 Publications6
Nucleotide bindingi57 – 59AMPUniRule annotation2 Publications3
Nucleotide bindingi85 – 88AMPUniRule annotation2 Publications4
Nucleotide bindingi136 – 137ATPUniRule annotation2 Publications2

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

BioCyciBSUB:BSU01370-MONOMER.
BRENDAi2.7.4.3. 658.
SABIO-RKP16304.
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
Superoxide-inducible protein 16
Short name:
SOI16
Gene namesi
Name:adkUniRule annotation
Ordered Locus Names:BSU01370
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001587301 – 217Adenylate kinaseAdd BLAST217

Proteomic databases

PaxDbiP16304.
PRIDEiP16304.

Expressioni

Inductioni

By superoxide.

Interactioni

Subunit structurei

Monomer.UniRule annotation1 Publication

Protein-protein interaction databases

IntActiP16304. 1 interactor.
MINTiMINT-8366209.
STRINGi224308.Bsubs1_010100000705.

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 – 53Combined sources10
Turni54 – 56Combined sources3
Helixi61 – 72Combined sources12
Helixi75 – 77Combined sources3
Beta strandi81 – 85Combined sources5
Helixi90 – 102Combined sources13
Beta strandi109 – 114Combined sources6
Helixi117 – 124Combined sources8
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 – 188Combined sources24
Beta strandi192 – 196Combined sources5
Helixi201 – 212Combined sources12
Helixi213 – 215Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1P3JX-ray1.90A1-217[»]
2EU8X-ray1.80A/B1-216[»]
2OO7X-ray1.80A/B1-217[»]
2ORIX-ray1.80A/B1-216[»]
2OSBX-ray1.80A/B1-216[»]
2P3SX-ray1.80A1-217[»]
2QAJX-ray1.80A/B1-217[»]
3DKVX-ray1.82A1-217[»]
3DL0X-ray1.58A/B1-216[»]
4MKFX-ray1.70A/B1-217[»]
4MKGX-ray1.45A1-217[»]
4MKHX-ray1.50A1-212[»]
4QBFX-ray1.80A1-217[»]
4QBGX-ray1.37B1-217[»]
4TYPX-ray2.90A/B/C/D1-217[»]
4TYQX-ray1.65A/B1-217[»]
ProteinModelPortaliP16304.
SMRiP16304.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16304.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni30 – 59NMPbindUniRule annotation2 PublicationsAdd BLAST30
Regioni126 – 163LIDUniRule annotation2 PublicationsAdd 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 annotation3 Publications

Sequence similaritiesi

Belongs to the adenylate kinase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0563. LUCA.
HOGENOMiHOG000238772.
InParanoidiP16304.
KOiK00939.
OMAiPHISTGA.
PhylomeDBiP16304.

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.

P16304-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:217
Mass (Da):24,119
Last modified:February 1, 1991 - v2
Checksum:iECB9ECF4F26A1E90
GO

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.
PIRiJS0492.
RefSeqiNP_388018.1. NC_000964.3.
WP_004399686.1. NZ_JNCM01000029.1.

Genome annotation databases

EnsemblBacteriaiCAB11913; CAB11913; BSU01370.
GeneIDi938508.
KEGGibsu:BSU01370.
PATRICi18971783. VBIBacSub10457_0140.

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.
PIRiJS0492.
RefSeqiNP_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 entryMethodResolution (Å)ChainPositionsPDBsum
1P3JX-ray1.90A1-217[»]
2EU8X-ray1.80A/B1-216[»]
2OO7X-ray1.80A/B1-217[»]
2ORIX-ray1.80A/B1-216[»]
2OSBX-ray1.80A/B1-216[»]
2P3SX-ray1.80A1-217[»]
2QAJX-ray1.80A/B1-217[»]
3DKVX-ray1.82A1-217[»]
3DL0X-ray1.58A/B1-216[»]
4MKFX-ray1.70A/B1-217[»]
4MKGX-ray1.45A1-217[»]
4MKHX-ray1.50A1-212[»]
4QBFX-ray1.80A1-217[»]
4QBGX-ray1.37B1-217[»]
4TYPX-ray2.90A/B/C/D1-217[»]
4TYQX-ray1.65A/B1-217[»]
ProteinModelPortaliP16304.
SMRiP16304.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP16304. 1 interactor.
MINTiMINT-8366209.
STRINGi224308.Bsubs1_010100000705.

Proteomic databases

PaxDbiP16304.
PRIDEiP16304.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB11913; CAB11913; BSU01370.
GeneIDi938508.
KEGGibsu:BSU01370.
PATRICi18971783. VBIBacSub10457_0140.

Phylogenomic databases

eggNOGiCOG0563. LUCA.
HOGENOMiHOG000238772.
InParanoidiP16304.
KOiK00939.
OMAiPHISTGA.
PhylomeDBiP16304.

Enzyme and pathway databases

UniPathwayiUPA00588; UER00649.
BioCyciBSUB:BSU01370-MONOMER.
BRENDAi2.7.4.3. 658.
SABIO-RKP16304.

Miscellaneous databases

EvolutionaryTraceiP16304.

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_BACSU
AccessioniPrimary (citable) accession number: P16304
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 1, 1991
Last modified: November 30, 2016
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.