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

ADK1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways.UniRule annotation3 Publications

Catalytic activityi

ATP + AMP = 2 ADP.UniRule annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei37AMPUniRule annotation2 Publications1
Binding sitei42AMPUniRule annotation2 Publications1
Binding sitei99AMPUniRule annotation2 Publications1
Binding sitei134ATPUniRule annotation3 Publications1
Binding sitei167AMPUniRule annotation2 Publications1
Binding sitei178AMPUniRule annotation2 Publications1
Binding sitei206ATP; via carbonyl oxygenUniRule annotation3 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi16 – 21ATPUniRule annotation3 Publications6
Nucleotide bindingi63 – 65AMPUniRule annotation2 Publications3
Nucleotide bindingi92 – 95AMPUniRule annotation2 Publications4
Nucleotide bindingi143 – 144ATP3 Publications2

GO - Molecular functioni

  • adenylate kinase activity Source: SGD
  • ATP binding Source: UniProtKB-KW

GO - Biological processi

  • ADP biosynthetic process Source: SGD
  • AMP metabolic process Source: UniProtKB-HAMAP
  • ATP metabolic process Source: UniProtKB-HAMAP
  • DNA replication initiation Source: SGD
  • nucleotide metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:YDR226W-MONOMER.
YEAST:YDR226W-MONOMER.
ReactomeiR-SCE-499943. Synthesis and interconversion of nucleotide di- and triphosphates.
SABIO-RKP07170.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate kinaseUniRule annotation (EC:2.7.4.3UniRule annotation)
Alternative name(s):
ATP-AMP transphosphorylaseUniRule annotation
ATP:AMP phosphotransferaseUniRule annotation
Adenylate kinase cytosolic and mitochondrialUniRule annotation
Adenylate monophosphate kinaseUniRule annotation
Gene namesi
Name:ADK1UniRule annotation
Synonyms:AKY, AKY1, AKY2
Ordered Locus Names:YDR226W
ORF Names:YD9934.11
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR226W.
SGDiS000002634. ADK1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • cytosol Source: UniProtKB-SubCell
  • mitochondrial intermembrane space Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Disruption phenotypei

The phenotype of disruption mutants is pet, showing that complementation by another adenylate kinase isozyme occurs only under fermentative conditions. The disruption completely destroys the activity in mitochondria, whereas in the cytoplasmic fraction about 10% is retained.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
PropeptideiPRO_00000165502Removed in mature formUniRule annotation1 Publication1
ChainiPRO_00000165513 – 222Adenylate kinaseAdd BLAST220

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei3N-acetylserineUniRule annotation1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP07170.
PRIDEiP07170.
TopDownProteomicsiP07170.

2D gel databases

SWISS-2DPAGEP07170.

PTM databases

iPTMnetiP07170.

Interactioni

Subunit structurei

Monomer.UniRule annotation3 Publications

Protein-protein interaction databases

BioGridi32278. 71 interactors.
DIPiDIP-5129N.
IntActiP07170. 4 interactors.
MINTiMINT-501634.

Structurei

Secondary structure

1222
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 12Combined sources5
Helixi19 – 30Combined sources12
Beta strandi33 – 36Combined sources4
Helixi37 – 46Combined sources10
Helixi50 – 60Combined sources11
Helixi67 – 80Combined sources14
Helixi82 – 85Combined sources4
Beta strandi88 – 92Combined sources5
Helixi97 – 110Combined sources14
Beta strandi116 – 121Combined sources6
Helixi124 – 132Combined sources9
Beta strandi134 – 136Combined sources3
Turni138 – 140Combined sources3
Beta strandi143 – 145Combined sources3
Turni146 – 148Combined sources3
Turni158 – 160Combined sources3
Helixi172 – 185Combined sources14
Helixi188 – 195Combined sources8
Beta strandi199 – 203Combined sources5
Helixi208 – 219Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AKYX-ray1.63A3-221[»]
1DVRX-ray2.36A/B3-221[»]
2AKYX-ray1.96A3-221[»]
3AKYX-ray2.23A3-221[»]
ProteinModelPortaliP07170.
SMRiP07170.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07170.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni36 – 65NMPbindUniRule annotation2 PublicationsAdd BLAST30
Regioni133 – 170LIDUniRule 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.UniRule annotation3 Publications

Sequence similaritiesi

Belongs to the adenylate kinase family. AK2 subfamily.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00830000128340.
HOGENOMiHOG000238772.
InParanoidiP07170.
KOiK00939.
OMAiNNKECQG.
OrthoDBiEOG092C5OQU.

Family and domain databases

CDDicd01428. ADK. 1 hit.
Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk. 1 hit.
MF_03168. Adenylate_kinase_AK2. 1 hit.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR033690. Adenylat_kinase_CS.
IPR007862. Adenylate_kinase_lid-dom.
IPR028587. AK2.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07170-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSESIRMV LIGPPGAGKG TQAPNLQERF HAAHLATGDM LRSQIAKGTQ
60 70 80 90 100
LGLEAKKIMD QGGLVSDDIM VNMIKDELTN NPACKNGFIL DGFPRTIPQA
110 120 130 140 150
EKLDQMLKEQ GTPLEKAIEL KVDDELLVAR ITGRLIHPAS GRSYHKIFNP
160 170 180 190 200
PKEDMKDDVT GEALVQRSDD NADALKKRLA AYHAQTEPIV DFYKKTGIWA
210 220
GVDASQPPAT VWADILNKLG KD
Length:222
Mass (Da):24,255
Last modified:July 1, 1989 - v2
Checksum:iFE566FD8015907CE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti95R → K in AAS56904 (PubMed:17322287).Curated1
Sequence conflicti139A → R in CAA68471 (PubMed:2821496).Curated1
Sequence conflicti222D → N AA sequence (PubMed:3004985).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06304 Genomic DNA. Translation: CAA29624.1.
Y00413 mRNA. Translation: CAA68471.1.
M18455 Genomic DNA. Translation: AAA66319.1.
U13239 Genomic DNA. Translation: AAC33143.1.
Z48612 Genomic DNA. Translation: CAA88506.1.
AY558578 Genomic DNA. Translation: AAS56904.1.
BK006938 Genomic DNA. Translation: DAA12068.1.
PIRiS05799. KIBYA.
RefSeqiNP_010512.1. NM_001180534.1.

Genome annotation databases

EnsemblFungiiYDR226W; YDR226W; YDR226W.
GeneIDi851812.
KEGGisce:YDR226W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06304 Genomic DNA. Translation: CAA29624.1.
Y00413 mRNA. Translation: CAA68471.1.
M18455 Genomic DNA. Translation: AAA66319.1.
U13239 Genomic DNA. Translation: AAC33143.1.
Z48612 Genomic DNA. Translation: CAA88506.1.
AY558578 Genomic DNA. Translation: AAS56904.1.
BK006938 Genomic DNA. Translation: DAA12068.1.
PIRiS05799. KIBYA.
RefSeqiNP_010512.1. NM_001180534.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AKYX-ray1.63A3-221[»]
1DVRX-ray2.36A/B3-221[»]
2AKYX-ray1.96A3-221[»]
3AKYX-ray2.23A3-221[»]
ProteinModelPortaliP07170.
SMRiP07170.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32278. 71 interactors.
DIPiDIP-5129N.
IntActiP07170. 4 interactors.
MINTiMINT-501634.

PTM databases

iPTMnetiP07170.

2D gel databases

SWISS-2DPAGEP07170.

Proteomic databases

MaxQBiP07170.
PRIDEiP07170.
TopDownProteomicsiP07170.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR226W; YDR226W; YDR226W.
GeneIDi851812.
KEGGisce:YDR226W.

Organism-specific databases

EuPathDBiFungiDB:YDR226W.
SGDiS000002634. ADK1.

Phylogenomic databases

GeneTreeiENSGT00830000128340.
HOGENOMiHOG000238772.
InParanoidiP07170.
KOiK00939.
OMAiNNKECQG.
OrthoDBiEOG092C5OQU.

Enzyme and pathway databases

BioCyciMetaCyc:YDR226W-MONOMER.
YEAST:YDR226W-MONOMER.
ReactomeiR-SCE-499943. Synthesis and interconversion of nucleotide di- and triphosphates.
SABIO-RKP07170.

Miscellaneous databases

EvolutionaryTraceiP07170.
PROiP07170.

Family and domain databases

CDDicd01428. ADK. 1 hit.
Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk. 1 hit.
MF_03168. Adenylate_kinase_AK2. 1 hit.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR033690. Adenylat_kinase_CS.
IPR007862. Adenylate_kinase_lid-dom.
IPR028587. AK2.
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 nameiKAD2_YEAST
AccessioniPrimary (citable) accession number: P07170
Secondary accession number(s): D6VSK8, Q6Q539
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: July 1, 1989
Last modified: November 30, 2016
This is version 184 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 123000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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.