Reviewed, UniProtKB/Swiss-Prot P07170 (KAD1_YEAST)

Names and origin

Protein names

Recommended name:
    Adenylate kinase 1
      Short name=AK 1
    EC=2.7.4.3
Alternative name(s):
    ATP-AMP transphosphorylase 1
    Adenylate kinase cytosolic and mitochondrial

Gene names

Name:	ADK1
Synonyms:	AKY, AKY1, AKY2
Ordered Locus Names:	YDR226W
ORF Names:	YD9934.11

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	222 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Small ubiquitous enzyme involved in energy metabolism and nucleotide synthesis that is essential for maintenance and cell growth. Functions both in the cytoplasm and mitochondrion intermembrane space.
Catalytic activity	ATP + AMP = 2 ADP.
Subunit structure	Monomer.
Subcellular location	Cytoplasm › cytosol. Mitochondrion intermembrane space Ref.8.
Miscellaneous	Present with 123000 molecules/cell in log phase SD medium. Ref.9
Sequence similarities	Belongs to the adenylate kinase family. AK2 subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm Mitochondrion
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	ADP biosynthetic process Ref.3 Inferred from direct assay. Source: SGD
Cellular component	cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial intermembrane space Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylate kinase activity Inferred from direct assay. Source: SGD identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-9447,EBI-9447
	P43582	1	EBI-9447,EBI-22766
RSP5	P39940	1	EBI-9447,EBI-16219
UBC1	P21734	1	EBI-9447,EBI-19717
VID30	P53076	1	EBI-9447,EBI-24173

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 2

2

Removed in mature form

PRO_0000016550

Chain

3 – 222

220

Adenylate kinase 1

PRO_0000016551

Regions

Nucleotide binding

13 – 21

9

ATP

Nucleotide binding

92 – 99

8

AMP

Sites

Binding site

37

1

AMP

Amino acid modifications

Modified residue

3

1

N-acetylserine Ref.7

Modified residue

140

1

Phosphoserine Ref.10

Experimental info

Sequence conflict

95

1

R → K in AAS56904. Ref.6

Sequence conflict

139

1

A → R in CAA68471. Ref.2

Sequence conflict

222

1

D → N AA sequence Ref.7

Secondary structure

1

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222

Helix Strand Turn

Details...

Beta strand

8 – 12

5

Helix

19 – 30

12

Beta strand

33 – 36

4

Helix

37 – 46

10

Helix

50 – 58

9

Helix

59 – 61

3

Helix

68 – 80

13

Helix

82 – 85

4

Beta strand

88 – 92

5

Helix

97 – 110

14

Beta strand

115 – 121

7

Helix

124 – 132

9

Beta strand

134 – 137

4

Turn

138 – 141

4

Beta strand

142 – 145

4

Turn

146 – 148

3

Turn

158 – 160

3

Helix

172 – 195

24

Beta strand

199 – 203

5

Helix

208 – 218

11

Sequences

	Sequence		Length	Mass (Da)
	P07170-1 [UniParc]. Last modified July 1, 1989. Version 2. Checksum: FE566FD8015907CE	FASTA	222	24,255
	10 20 30 40 50 60 MSSSESIRMV LIGPPGAGKG TQAPNLQERF HAAHLATGDM LRSQIAKGTQ LGLEAKKIMD 70 80 90 100 110 120 QGGLVSDDIM VNMIKDELTN NPACKNGFIL DGFPRTIPQA EKLDQMLKEQ GTPLEKAIEL 130 140 150 160 170 180 KVDDELLVAR ITGRLIHPAS GRSYHKIFNP PKEDMKDDVT GEALVQRSDD NADALKKRLA 190 200 210 220 AYHAQTEPIV DFYKKTGIWA GVDASQPPAT VWADILNKLG KD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2834097] [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: 2821496] [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: 2848829] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Insertion site specificity of the transposon Tn3." Davies C.J., Hutchison C.A. III Nucleic Acids Res. 23:507-514(1995) [PubMed: 7885847] [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: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[6]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[7]	"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: 3004985] [Abstract] Cited for: PROTEIN SEQUENCE OF 3-222.
[8]	"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: 12045196] [Abstract] Cited for: SUBCELLULAR LOCATION.
[9]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, MASS SPECTROMETRY.
[11]	"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: 7670369] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
[12]	"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: 8594191] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 3-221 IN COMPLEX WITH ATP ANALOG.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

KIBYA. S05799.

RefSeq

NP_010512.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AKY	X-ray	1.63	A	3-221	[»]
1DVR	X-ray	2.36	A/B	3-221	[»]
2AKY	X-ray	1.96	A	3-221	[»]
3AKY	X-ray	2.23	A	3-221	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5129N.

IntAct

P07170. 15 interactions.

STRING

P07170.

2-D gel databases

SWISS-2DPAGE

P07170.

Proteomic databases

PeptideAtlas

P07170.

PRIDE

P07170.

Genome annotation databases

Ensembl

YDR226W; YDR226W; YDR226W; Saccharomyces cerevisiae. [Genome view]

GeneID

851812.

KEGG

sce:YDR226W.

NMPDR

fig|4932.3.peg.1269.

Organism-specific databases

CYGD

YDR226w.

SGD

S000002634. ADK1.

Phylogenomic databases

eggNOG

fuNOG05172.

HOGENOM

HBG630208.

OMA

MVLIGPP.

OrthoDB

EOG95DZ5W.

PhylomeDB

P07170.

Enzyme and pathway databases

BRENDA

2.7.4.3. 250.

Gene expression databases

ArrayExpress

P07170.

Genevestigator

P07170.

GermOnline

YDR226W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR006259. Adenyl_kin_sub.
IPR000850. Adenylate_kin.
IPR007862. Adenylate_kinase_lid-dom.
[Graphical view]

PANTHER

PTHR23359. Adenylate_kin. 1 hit.

Pfam

PF00406. ADK. 1 hit.
PF05191. ADK_lid. 1 hit.
[Graphical view]

PRINTS

PR00094. ADENYLTKNASE.

TIGRFAMs

TIGR01351. adk. 1 hit.

PROSITE

PS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

969668.

Entry information

Entry name

KAD1_YEAST

Accession

Primary (citable) accession number: P07170
Secondary accession number(s): Q6Q539

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	July 1, 1989
Last modified:	February 9, 2010
This is version 119 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)