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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei37 – 371AMPUniRule annotation2 Publications
Binding sitei42 – 421AMPUniRule annotation2 Publications
Binding sitei99 – 991AMPUniRule annotation2 Publications
Binding sitei134 – 1341ATPUniRule annotation3 Publications
Binding sitei167 – 1671AMPUniRule annotation2 Publications
Binding sitei178 – 1781AMPUniRule annotation2 Publications
Binding sitei206 – 2061ATP; via carbonyl oxygenUniRule annotation3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi16 – 216ATPUniRule annotation3 Publications
Nucleotide bindingi63 – 653AMPUniRule annotation2 Publications
Nucleotide bindingi92 – 954AMPUniRule annotation2 Publications
Nucleotide bindingi143 – 1442ATP3 Publications

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Propeptidei2 – 21Removed in mature formUniRule annotation1 PublicationPRO_0000016550
Chaini3 – 222220Adenylate kinasePRO_0000016551Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei3 – 31N-acetylserineUniRule annotation1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP07170.
TopDownProteomicsiP07170.

2D gel databases

SWISS-2DPAGEP07170.

PTM databases

iPTMnetiP07170.

Interactioni

Subunit structurei

Monomer.UniRule annotation3 Publications

Protein-protein interaction databases

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

Structurei

Secondary structure

1
222
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 125Combined sources
Helixi19 – 3012Combined sources
Beta strandi33 – 364Combined sources
Helixi37 – 4610Combined sources
Helixi50 – 6011Combined sources
Helixi67 – 8014Combined sources
Helixi82 – 854Combined sources
Beta strandi88 – 925Combined sources
Helixi97 – 11014Combined sources
Beta strandi116 – 1216Combined sources
Helixi124 – 1329Combined sources
Beta strandi134 – 1363Combined sources
Turni138 – 1403Combined sources
Beta strandi143 – 1453Combined sources
Turni146 – 1483Combined sources
Turni158 – 1603Combined sources
Helixi172 – 18514Combined sources
Helixi188 – 1958Combined sources
Beta strandi199 – 2035Combined sources
Helixi208 – 21912Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKYX-ray1.63A3-221[»]
1DVRX-ray2.36A/B3-221[»]
2AKYX-ray1.96A3-221[»]
3AKYX-ray2.23A3-221[»]
ProteinModelPortaliP07170.
SMRiP07170. Positions 5-222.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07170.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni36 – 6530NMPbindUniRule annotation2 PublicationsAdd
BLAST
Regioni133 – 17038LIDUniRule 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.UniRule annotation3 Publications

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00830000128340.
HOGENOMiHOG000238772.
InParanoidiP07170.
KOiK00939.
OMAiKEKFSCC.
OrthoDBiEOG7BCNPJ.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
MF_03168. Adenylate_kinase_AK2.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951R → K in AAS56904 (PubMed:17322287).Curated
Sequence conflicti139 – 1391A → R in CAA68471 (PubMed:2821496).Curated
Sequence conflicti222 – 2221D → N AA sequence (PubMed:3004985).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKYX-ray1.63A3-221[»]
1DVRX-ray2.36A/B3-221[»]
2AKYX-ray1.96A3-221[»]
3AKYX-ray2.23A3-221[»]
ProteinModelPortaliP07170.
SMRiP07170. Positions 5-222.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP07170.

2D gel databases

SWISS-2DPAGEP07170.

Proteomic databases

MaxQBiP07170.
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.
OMAiKEKFSCC.
OrthoDBiEOG7BCNPJ.

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

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
MF_03168. Adenylate_kinase_AK2.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
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...

Publicationsi

« Hide 'large scale' publications
  1. "The complete nucleotide sequence of the gene coding for yeast adenylate kinase."
    Magdolen V., Oechsner U., Bandlow W.
    Curr. Genet. 12:405-411(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The cDNA sequence encoding cytosolic adenylate kinase from baker's yeast (Saccharomyces cerevisiae)."
    Proba K., Tomasselli A.G., Nielsen P., Schulz G.E.
    Nucleic Acids Res. 15:7187-7187(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Analysis and in vivo disruption of the gene coding for adenylate kinase (ADK1) in the yeast Saccharomyces cerevisiae."
    Konrad M.
    J. Biol. Chem. 263:19468-19474(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  4. "Insertion site specificity of the transposon Tn3."
    Davies C.J., Hutchison C.A. III
    Nucleic Acids Res. 23:507-514(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  7. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  8. "The complete amino acid sequence of adenylate kinase from baker's yeast."
    Tomasselli A.G., Mast E., Janes W., Schiltz E.
    Eur. J. Biochem. 155:111-119(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 3-222, ACETYLATION [LARGE SCALE ANALYSIS] AT SER-3.
  9. "Yeast adenylate kinase is active simultaneously in mitochondria and cytoplasm and is required for non-fermentative growth."
    Bandlow W., Strobel G., Zoglowek C., Oechsner U., Magdolen V.
    Eur. J. Biochem. 178:451-457(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  10. "Redundant mitochondrial targeting signals in yeast adenylate kinase."
    Schricker R., Angermayr M., Strobel G., Klinke S., Korber D., Bandlow W.
    J. Biol. Chem. 277:28757-28764(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  12. "Co-regulation of yeast purine and phosphate pathways in response to adenylic nucleotide variations."
    Gauthier S., Coulpier F., Jourdren L., Merle M., Beck S., Konrad M., Daignan-Fornier B., Pinson B.
    Mol. Microbiol. 68:1583-1594(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Stability, activity and structure of adenylate kinase mutants."
    Spuergin P., Abele U., Schulz G.E.
    Eur. J. Biochem. 231:405-413(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 3-221 IN COMPLEX WITH BI-SUBSTRATE ANALOG AP5A.
  16. "High-resolution structures of adenylate kinase from yeast ligated with inhibitor Ap5A, showing the pathway of phosphoryl transfer."
    Abele U., Schulz G.E.
    Protein Sci. 4:1262-1271(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) IN COMPLEX WITH BI-SUBSTRATE ANALOG AP5A.
  17. "Structure of a mutant adenylate kinase ligated with an ATP-analogue showing domain closure over ATP."
    Schlauderer G.J., Proba K., Schulz G.E.
    J. Mol. Biol. 256:223-227(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 3-221 IN COMPLEX WITH ATP ANALOG.

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: July 6, 2016
This is version 180 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.