Q7QJX9 (KAD2_ANOGA) Reviewed, UniProtKB/Swiss-Prot

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

Gene names

Name:	Adk2
ORF Names:	AGAP007722

Organism

Anopheles gambiae (African malaria mosquito)

Taxonomic identifier

7165 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicoidea › Culicidae › Anophelinae › Anopheles

Protein attributes

Sequence length	240 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 Reference proteome
Gene Ontology (GO)
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 – 240	240	Adenylate kinase 2, mitochondrial		PRO_0000365701
Regions
	Nucleotide binding	25 – 33	9	ATP By similarity
	Nucleotide binding	48 – 77	30	AMP By similarity
Sites
	Binding site	49	1	AMP By similarity
Amino acid modifications
	Disulfide bond	45 ↔ 95		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7QJX9 [UniParc]. Last modified December 7, 2004. Version 2. Checksum: 6A17E80EC4FAE8DE	FASTA	240	26,431
	10 20 30 40 50 60 MAPNAAELKV KPASDSTGIN AILLGPPGSG KGTQAPLLKE KYCVCHLSTG DMLRAEIASG 70 80 90 100 110 120 SKLGAQLKKV MDEGKLVSDE LVVDMIDSNL DKPECRNGFL LDGFPRTVVQ AEKLDNLLEK 130 140 150 160 170 180 RNTGLDAVIE FGIDDSLLVR RITGRLIHQA SGRSYHEEFA PPKVPMRDDE TGEPLMRRSD 190 200 210 220 230 240 DNAQALVKRL ESYHRQTKPL ADYYALRGLH FRVDAAKSAS DVFANIDSIF TKQRAHRLGF

References

[1]

"The genome sequence of the malaria mosquito Anopheles gambiae." Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R., Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z., Kraft C.L., Abril J.F. , Anthouard V., Arensburger P., Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K., Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I., Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I., Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I., Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C., Collins F.H., Hoffman S.L. Science 298:129-149(2002) [PubMed: 12364791] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PEST.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAAB01008807 Genomic DNA. Translation: EAA04739.2.
RefSeq	XP_308155.2. XM_308155.4.
3D structure databases
HSSP	HSSP built from PDB template 2C9Y based on UniProtKB P54819.
ProteinModelPortal	Q7QJX9.
SMR	Q7QJX9. Positions 18-232.
ModBase	Search...
Protein-protein interaction databases
STRING	Q7QJX9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	AGAP007722-RA; AGAP007722-PA; AGAP007722.
GeneID	1269521.
KEGG	aga:AgaP_AGAP007722.
VectorBase	AGAP007722. Anopheles gambiae.
Organism-specific databases
CTD	1269521.
Phylogenomic databases
eggNOG	inNOG04513.
GeneTree	EMGT00050000010442.
HOGENOM	HBG630208.
OMA	HEEFHPP.
OrthoDB	EOG43BK4X.
PhylomeDB	Q7QJX9.
Family and domain databases
InterPro	IPR006259. Adenyl_kin_sub. IPR000850. Adenylate_kin. IPR007862. Adenylate_kinase_lid-dom. [Graphical view]
KO	K00939.
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_ANOGA

Accession

Primary (citable) accession number: Q7QJX9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 3, 2009
Last sequence update:	December 7, 2004
Last modified:	December 14, 2011
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)