O49923 (ADK_PHYPA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Adenosine 5'-phosphotransferase

Gene names

Name:	ADK
ORF Names:	PHYPADRAFT_184505

Organism

Physcomitrella patens subsp. patens (Moss)

Taxonomic identifier

145481 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Bryophyta › Bryophytina › Bryopsida › Funariidae › Funariales › Funariaceae › Physcomitrella

Protein attributes

Sequence length	343 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. Can also act on the cytokinin isopentenyladenosine to produce isopentenyladenosine monophosphate. Ref.1
Catalytic activity	ATP + adenosine = ADP + AMP.
Cofactor	Magnesium By similarity.
Pathway	Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1.
Sequence similarities	Belongs to the carbohydrate kinase pfkB family.

Ontologies

Keywords
Biological process	Purine salvage
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	purine ribonucleoside salvage Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenosine kinase activity Inferred from electronic annotation. Source: EC 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 – 343	343	Adenosine kinase		PRO_0000080059
Sites
	Active site	296	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	O49923 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: E29FEC383795E543	FASTA	343	37,251
	10 20 30 40 50 60 MASEGVLLGM GNPLLDISCV VDDAFLEKYG LTLNNAILAE DKHLPMYKEL AANPDVEYIA 70 80 90 100 110 120 GGATQNTIRI AQWMLGESNA TSYFGCVGKD EYGDRMFKLA SEGGVNIRYD VDEDLPTGTC 130 140 150 160 170 180 GVLVVKGERS LVANLSAANK YKIDHLKKPE NWAFVEKAKY IYSAGFFLTV SPESMMTVAK 190 200 210 220 230 240 HAAETGKYYM INLAAPFICQ FFKDPLMELF PYVDFIFGNE SEARAFAQVQ GWETEDTKVI 250 260 270 280 290 300 AVKLAALPKA GGTHKRVAVI TQGTDPTIVA EDGKVTEFPV TPIPKEKLVD TNAAGDSFVG 310 320 330 340 GFLSQLVLGK DIAQCVRAGN YAASVIIQRS GCTFPSKPSF ESQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of an adenosine kinase from Physcomitrella involved in cytokinin metabolism." von Schwartzenberg K., Kruse S., Reski R., Moffatt B., Laloue M. Plant J. 13:249-257(1998) [PubMed: 9680981] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. Strain: Cambridge.
[2]	"The Physcomitrella genome reveals evolutionary insights into the conquest of land by plants." Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H., Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T., Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A., Suzuki Y. , Hashimoto S., Yamaguchi K., Sugano A., Kohara Y., Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E., Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M., Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J., Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B., Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A., Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y., Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M., Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S., Boore J.L. Science 319:64-69(2008) [PubMed: 18079367] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y15430 mRNA. Translation: CAA75628.1. DS544963 Genomic DNA. Translation: EDQ69929.1.
RefSeq	XP_001765201.1. XM_001765149.1.
UniGene	Ppa.45.
3D structure databases
ProteinModelPortal	O49923.
SMR	O49923. Positions 3-341.
ModBase	Search...
Protein-protein interaction databases
STRING	O49923.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	ESTEXT_GWP_GW1.C_740114; ESTEXT_GWP_GW1.C_740114; ESTEXT_GWP_GW1.C_740114.
GeneID	5928421.
KEGG	ppp:PHYPADRAFT_184505.
Phylogenomic databases
GeneTree	EPGT00050000007167.
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

ADK_PHYPA

Accession

Primary (citable) accession number: O49923
Secondary accession number(s): A9SFV8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 16, 2001
Last sequence update:	June 1, 1998
Last modified:	January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program