Reviewed, UniProtKB/Swiss-Prot Q54QJ9 (KAD2_DICDI)

Names and origin

Protein names

Recommended name:
    Adenylate kinase 2, mitochondrial
      Short name=AK 2
    EC=2.7.4.3
Alternative name(s):
    ATP-AMP transphosphorylase 2
    Adenylate kinase A

Gene names

Name:	adkA
ORF Names:	DDB_G0283805

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	276 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. This small ubiquitous enzyme involved in energy metabolism and nucleotide synthesis that is essential for maintenance and cell growth By similarity.
Catalytic activity	ATP + AMP = 2 ADP.
Subunit structure	Monomer By similarity.
Subcellular location	Mitochondrion intermembrane space By similarity.
Sequence similarities	Belongs to the adenylate kinase family. AK2 subfamily.

Ontologies

Keywords
Cellular component	Mitochondrion
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	nucleobase, nucleoside, nucleotide and nucleic acid metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial intermembrane space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylate kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 276	276	Adenylate kinase 2, mitochondrial		PRO_0000342150
Regions
	Nucleotide binding	35 – 43	9	ATP By similarity
	Nucleotide binding	58 – 87	30	AMP By similarity
Sites
	Binding site	59	1	AMP By similarity
Amino acid modifications
	Disulfide bond	55 ↔ 105		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54QJ9-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: A60FE1596D50AEA9	FASTA	276	30,985
	10 20 30 40 50 60 MEPQFKVKID NDSARILKEL AEKKRDEGLR VVFIGPPGSG KGTQAPLVKE DYCLCHLSTG 70 80 90 100 110 120 DMLRAAIEQG TETGKQAKTI MDQGGLVPDE VMVNMIKENI QTPECKKGFI LDGFPRTVPQ 130 140 150 160 170 180 AEKLDKMLAE DNKKIDHVLD FAIDDSLLVK RITGRLVHPS SGRSYHREFF PPKVDMIDDI 190 200 210 220 230 240 TGEPLIQRSD DNEEVLKKRL ESFHKNTTPV LGYYQNKGIL STIDASKSAP FVSHTIKSIF 250 260 270 LSTLHFPHNA SIFKTFHQKM KMQVHSTETP LAAEIL

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000057 Genomic DNA. Translation: EAL65517.1.
RefSeq	XP_638872.1.
3D structure databases
HSSP	HSSP built from PDB template 2C9Y based on UniProtKB P54819.
SMR	Q54QJ9. Positions 29-239.
ModBase	Search...
Protein-protein interaction databases
STRING	Q54QJ9.
Genome annotation databases
GeneID	8624270.
KEGG	ddi:DDB_0230096.
Organism-specific databases
dictyBase	DDB_G0283805. adkA.
Phylogenomic databases
eggNOG	KOG3078.
HOGENOM	HBG630208.
OMA	MVLIGPP.
PhylomeDB	Q54QJ9.
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...

Entry information

Entry name

KAD2_DICDI

Accession

Primary (citable) accession number: Q54QJ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 2008
Last sequence update:	May 24, 2005
Last modified:	February 9, 2010
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)