Q9LZG0 (ADK2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adenosine kinase 2
Short name=AK 2
EC=2.7.1.20

Alternative name(s):
Adenosine 5'-phosphotransferase 2

Gene names

Name:	ADK2
Ordered Locus Names:	At5g03300
ORF Names:	F12E4.30, MOK16.21

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	345 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. Essential to sustain methyl recycling. Ref.7
Catalytic activity	ATP + adenosine = ADP + AMP.
Cofactor	Magnesium By similarity.
Enzyme regulation	Inactivated by the begomovirus AL2 protein or the curtovirus L2 protein. Ref.6
Pathway	Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1.
Subunit structure	Interacts with the begomovirus AL2 protein and the curtovirus L2 protein. Ref.6
Tissue specificity	Ubiquitous. Ref.1 Ref.7
Developmental stage	Up-regulated during the lignification process in inflorescence stems. Ref.7
Sequence similarities	Belongs to the carbohydrate kinase pfkB family.

Ontologies

Keywords
Biological process	Host-virus interaction Purine salvage
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	adenosine salvage Traceable author statement Ref.1. Source: TAIR interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: TAIR plasma membrane Inferred from direct assay. Source: TAIR
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenosine kinase activity Inferred from direct assay Ref.1. Source: TAIR copper ion binding Inferred from direct assay. Source: TAIR phosphotransferase activity, alcohol group as acceptor Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 345	345	Adenosine kinase 2		PRO_0000080058
Sites
	Active site	300	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9LZG0 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 0834B163049F740E	FASTA	345	37,846
	10 20 30 40 50 60 MASSSNYDGI LLGMGNPLLD ISAVVDDEFL TKYDIKLNNA ILAEDKHLPM YDEMSSKFNV 70 80 90 100 110 120 EYIAGGATQN SIKVAQWMLQ IPGATSYMGS IGKDKYGEAM KKDATAAGVN VHYYEDESAP 130 140 150 160 170 180 TGTCGVCVVG GERSLIANLS AANCYKVDHL KKPENWALVE KAKFYYIAGF FLTVSPESIQ 190 200 210 220 230 240 LVSEHAAANN KVFTMNLSAP FICEFFKDVQ EKFLPYMDFV FGNETEARTF SRVHGWETED 250 260 270 280 290 300 VEQIAIKISQ LPKATGTYKR TTVITQGADP VVVAEDGKVK KYPVIPLPKE KLVDTNGAGD 310 320 330 340 AFVGGFMSQL VKEKSIEECV KAGCYASNVV IQRSGCTYPE KPDFN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Adenosine kinase of Arabidopsis. Kinetic properties and gene expression." Moffatt B.A., Wang L., Allen M.S., Stevens Y.Y., Qin W., Snider J., von Schwartzenberg K. Plant Physiol. 124:1775-1785(2000) [PubMed: 11115893] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, CHARACTERIZATION. Strain: cv. Columbia.
[2]	"Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence features of the 1.6 Mb regions covered by twenty physically assigned P1 clones." Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., Miyajima N., Tabata S. DNA Res. 4:215-230(1997) [PubMed: 9330910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F. Nature 408:823-826(2000) [PubMed: 11130714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Adenosine kinase is inactivated by geminivirus AL2 and L2 proteins." Wang H., Hao L., Shung C.-Y., Sunter G., Bisaro D.M. Plant Cell 15:3020-3032(2003) [PubMed: 14615595] [Abstract] Cited for: INTERACTION WITH TOMATO GOLDEN MOSAIC VIRUS AL2 AND BEET CURLY TOP VIRUS L2, ENZYME REGULATION.
[7]	"Methyl recycling activities are co-ordinately regulated during plant development." Pereira L.A.R., Todorova M., Cai X., Makaroff C.A., Emery R.J.N., Moffatt B.A. J. Exp. Bot. 58:1083-1098(2007) [PubMed: 17272833] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF180895 mRNA. Translation: AAG45247.1. AF180897 Genomic DNA. Translation: AAG45249.1. AB005240 Genomic DNA. Translation: BAB08390.1. AL162751 Genomic DNA. Translation: CAB83286.1. CP002688 Genomic DNA. Translation: AED90582.1. AY042855 mRNA. Translation: AAK68795.1. AY072485 mRNA. Translation: AAL66900.1.
IPI	IPI00523164.
PIR	T48351.
RefSeq	NP_195950.1. NM_120408.3.
UniGene	At.1599. At.16947.
3D structure databases
ProteinModelPortal	Q9LZG0.
SMR	Q9LZG0. Positions 7-345.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9LZG0. 1 interaction.
STRING	Q9LZG0.
Proteomic databases
PRIDE	Q9LZG0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G03300.1; AT5G03300.1; AT5G03300.
GeneID	831882.
GenomeReviews	Gene locus AT5G03300 in contig BA000015_GR.
KEGG	ath:AT5G03300.
NMPDR	fig|3702.1.peg.22411.
Organism-specific databases
TAIR	At5g03300.
Phylogenomic databases
eggNOG	KOG2854.
GeneTree	EPGT00050000007167.
HOGENOM	HBG314716.
InParanoid	Q9LZG0.
OMA	AQWMIQQ.
PhylomeDB	Q9LZG0.
ProtClustDB	PLN02548.
Enzyme and pathway databases
BRENDA	2.7.1.20. 399.
Gene expression databases
ArrayExpress	Q9LZG0.
Genevestigator	Q9LZG0.
GermOnline	AT5G03300. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR001805. Adenokinase. IPR011611. Carb/pur_kinase. IPR002173. Carboh/pur_kinase_PfkB_CS. [Graphical view]
KO	K00856.
PANTHER	PTHR10584:SF24. Adenokinase. 1 hit.
Pfam	PF00294. PfkB. 1 hit. [Graphical view]
PRINTS	PR00989. ADENOKINASE.
PROSITE	PS00583. PFKB_KINASES_1. False negative. PS00584. PFKB_KINASES_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ADK2_ARATH

Accession

Primary (citable) accession number: Q9LZG0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 16, 2001
Last sequence update:	October 1, 2000
Last modified:	December 14, 2011
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program