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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei31 – 311AMPUniRule annotation2 Publications
Binding sitei36 – 361AMPUniRule annotation2 Publications
Binding sitei92 – 921AMPUniRule annotation2 Publications
Binding sitei127 – 1271ATPUniRule annotation2 Publications
Metal bindingi130 – 1301Zinc; structuralUniRule annotation2 Publications
Metal bindingi133 – 1331Zinc; structuralUniRule annotation2 Publications
Metal bindingi150 – 1501Zinc; structuralUniRule annotation2 Publications
Metal bindingi153 – 1531Zinc; structuralUniRule annotation2 Publications
Binding sitei160 – 1601AMPUniRule annotation2 Publications
Binding sitei171 – 1711AMPUniRule annotation2 Publications
Binding sitei199 – 1991ATP; via carbonyl oxygenUniRule annotation2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 156ATPUniRule annotation2 Publications
Nucleotide bindingi57 – 593AMPUniRule annotation2 Publications
Nucleotide bindingi85 – 884AMPUniRule annotation2 Publications
Nucleotide bindingi136 – 1372ATPUniRule annotation2 Publications

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 217217Adenylate kinasePRO_0000158730Add
BLAST

Proteomic databases

PaxDbiP16304.

Expressioni

Inductioni

By superoxide.

Interactioni

Subunit structurei

Monomer.UniRule annotation1 Publication

Protein-protein interaction databases

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

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 – 5310Combined sources
Turni54 – 563Combined sources
Helixi61 – 7212Combined sources
Helixi75 – 773Combined sources
Beta strandi81 – 855Combined sources
Helixi90 – 10213Combined sources
Beta strandi109 – 1146Combined sources
Helixi117 – 1248Combined sources
Beta strandi127 – 1304Combined sources
Turni131 – 1333Combined sources
Beta strandi136 – 1383Combined sources
Turni139 – 1413Combined sources
Turni151 – 1533Combined sources
Beta strandi156 – 1583Combined sources
Helixi161 – 1633Combined sources
Helixi165 – 18824Combined sources
Beta strandi192 – 1965Combined sources
Helixi201 – 21212Combined sources
Helixi213 – 2153Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-216.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16304.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 5930NMPbindUniRule annotation2 PublicationsAdd
BLAST
Regioni126 – 16338LIDUniRule annotation2 PublicationsAdd
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 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.
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
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. Positions 1-216.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

PaxDbiP16304.

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.
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: September 7, 2016
This is version 147 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.