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InterPro: IPR000850 Adenylate kinase

Protein matches Help

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Matches:

3618 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR000850 Adenylate_kin

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00406	ADK	3340
PRINTS	PR00094	ADENYLTKNASE	3108
PROSITE pattern	PS00113	ADENYLATE_KINASE	2959
PANTHER	PTHR23359	Adenylate_kin	3531
Signatures in BioMart

InterPro Relationships Help

Children

IPR006259 Adenylate kinase, subfamily
IPR006266 UMP-CMP kinase
IPR006267 Adenylate kinase, isozyme 1

Contains

IPR007862 Adenylate kinase, active site lid domain

GO Term annotation Help

Process

GO:0006139 nucleobase, nucleoside, nucleotide and nucleic acid metabolic process

Function

GO:0005524 ATP binding
GO:0019205 nucleobase, nucleoside, nucleotide kinase activity

InterPro annotation

Entry Details in BioMart

Abstract

Adenylate kinases (ADK) are phosphotransferases that catalyse the reversible reaction

AMP + MgATP = ADP + MgADP

an essential reaction for many processes in living cells. Two ADK isozymes have been identified in mammalian cells. These specifically bind AMP and favour binding to ATP over other nucleotide triphosphates (AK1 is cytosolic and AK2 is located in the mitochondria). A third ADK has been identified in bovine heart and human cells [1], this is a mitochondrial GTP:AMP phosphotransferase, also specific for the phosphorylation of AMP, but can only use GTP or ITP as a substrate [2]. ADK has also been identified in different bacterial species and in yeast [3]. Two further enzymes are known to be related to the ADK family, i.e. yeast uridine monophosphokinase and slime mold UMP-CMP kinase. Within the ADK family there are several conserved regions, including the ATP-binding domains. One of the most conserved areas includes an Arg residue, whose modification inactivates the enzyme, together with an Asp that resides in the catalytic cleft of the enzyme and participates in a salt bridge.

Structural links Help

PDB - click here

SCOP: c.37.1.1 , g.41.2.1

CATH: 3.40.50.300

Database links Help

PDBe-motif: PS00113

Enzyme: EC:2.7.4.3

PROSITE doc: PDOC00104

PANDIT: PF00406

Blocks: IPB000850

Pfam Clan: CL0023.30

AC	CL0023.30
ID	AAA
DE	P-loop containing nucleoside triphosphate hydrolase superfamily
PF00004	IPR003959	ATPase, AAA-type, core
PF00005	IPR003439	ABC transporter-like
PF00158	IPR002078	RNA polymerase sigma factor 54, interaction
PF00265	IPR001267	Thymidine kinase
PF00308	IPR013317	Chromosomal replication control, initiator (DnaA)/regulator (Hda)
PF00406	IPR000850	Adenylate kinase
PF00437	IPR001482	Type II secretion system protein E
PF00485	IPR006083	Phosphoribulokinase/uridine kinase
PF00488	IPR000432	DNA mismatch repair protein MutS, C-terminal
PF00493	IPR001208	DNA-dependent ATPase MCM
PF00625	IPR008144	Guanylate kinase
PF00685	IPR000863	Sulfotransferase
PF00931	IPR002182	NB-ARC
PF01078	IPR000523	Magnesium chelatase, ChlI subunit
PF01202	IPR000623	Shikimate kinase
PF01580	IPR002543	Cell divisionFtsK/SpoIIIE
PF01583	IPR002891	Adenylylsulphate kinase, C-terminal
PF01637	IPR011579	ATPase domain, prokaryote
PF01656	IPR002586	Cobyrinic acid a,c-diamide synthase
PF01695	IPR002611	IstB-like ATP-binding protein
PF01712	IPR002624	Deoxynucleoside kinase
PF01715	IPR002627	tRNA isopentenyltransferase
PF01745	IPR002648	Isopentenyl transferase
PF01935	IPR002789	Protein of unknown function DUF87
PF02223	IPR000062	Thymidylate kinase-like
PF02224	IPR011994	Cytidylate kinase domain
PF02367	IPR003442	Uncharacterised protein family UPF0079, ATPase bacteria
PF02374	IPR003348	ATPase, anion-transporting
PF02463	IPR003395	RecF/RecN/SMC protein, N-terminal
PF02492	IPR003495	Cobalamin (vitamin B12) biosynthesis CobW-like
PF02534	IPR003688	TRAG protein
PF03205	IPR004435	Molybdopterin-guanine dinucleotide biosynthesis protein B (MobB), conserved region
PF03215	IPR004582	Checkpoint protein Rad24
PF03308	IPR005129	ArgK protein
PF03668	IPR005337	ATPase, P-loop-containing
PF03969	IPR005654	ATPase, AFG1-like
PF05621	IPR008868	Bacterial TniB
PF05707	IPR008900	Zonular occludens toxin
PF05729	IPR007111	NACHT nucleoside triphosphatase
PF05872	IPR008571	Protein of unknown function DUF853, nucleotide triphosphate hydrolase, putative
PF06068	IPR010339	TIP49, C-terminal
PF06144	IPR010372	DNA polymerase III, delta
PF06309	IPR010448	Torsin
PF06431	IPR010932	Large T antigen, polyomavirus, C-terminal
PF07693	IPR011646	KAP P-loop
PF07724	IPR013093	ATPase associated with various cellular activities, AAA-2
PF07726	IPR011703	ATPase associated with various cellular activities, AAA-3
PF07728	IPR011704	ATPase associated with various cellular activities, AAA-5
PF07931	IPR012853	Chloramphenicol phosphotransferase-like
PF08298	IPR013153	PrkA AAA
PF08433	IPR013641	Chromatin associated protein KTI12
PF08542	IPR013748	Replication factor C
PF10443	IPR018850	Mitochondrial escape protein 2, putative NTP-binding domain
PF10609	IPR019591	ATPase-like, ParA/MinD

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000850

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P00568 Adenylate kinase isoenzyme 1

P07170 Adenylate kinase 1

P34346 Adenylate kinase 2, mitochondrial

Q32M07 Putative adenylate kinase-like protein C9orf98 homolog

Q9U915 Adenylate kinase 2, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR006259	Adenylate kinase, subfamily
IPR000850	Adenylate kinase
IPR007862	Adenylate kinase, active site lid domain
IPR006267	Adenylate kinase, isozyme 1
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Wieland B, Tomasselli AG, Noda LH, Frank R, Schulz GE. The amino acid sequence of GTP:AMP phosphotransferase from beef-heart mitochondria. Extensive homology with cytosolic adenylate kinase. Eur. J. Biochem. 143 331-9 1984 [PubMed: 6088234] http://dx.doi.org/10.1111/j.1432-1033.1984.tb08376.x
2.	Tomasselli AG, Noda LH. Mitochondrial GTP-AMP phosphotransferase. 2. Kinetic and equilibrium dialysis studies. Eur. J. Biochem. 93 263-7 1979 [PubMed: 218813] http://dx.doi.org/10.1111/j.1432-1033.1979.tb12819.x
3.	Cooper AJ, Friedberg EC. A putative second adenylate kinase-encoding gene from the yeast Saccharomyces cerevisiae. Gene 114 145-8 1992 [PubMed: 1587477] http://dx.doi.org/10.1016/0378-1119(92)90721-Z

Additional Reading Open in usermanual
	Kath T, Schmid R, Schafer G. Identification, cloning, and expression of the gene for adenylate kinase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. Arch. Biochem. Biophys. 307 1993 405-10 [PubMed: 8274029] http://dx.doi.org/10.1006/abbi.1993.1607
	Schulz GE. Structural and functional relationships in the adenylate kinase family. Cold Spring Harb. Symp. Quant. Biol. 52 1987 429-39 [PubMed: 2841070]
	Liljelund P, Sanni A, Friesen JD, Lacroute F. Primary structure of the S. cerevisiae gene encoding uridine monophosphokinase. Biochem. Biophys. Res. Commun. 165 1989 464-73 [PubMed: 2556145] http://dx.doi.org/10.1016/0006-291X(89)91093-0
	Bae E, Phillips GN Jr. Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases. J. Biol. Chem. 279 2004 28202-8 [PubMed: 15100224] http://dx.doi.org/10.1074/jbc.M401865200
	Berry MB, Bae E, Bilderback TR, Glaser M, Phillips GN Jr. Crystal structure of ADP/AMP complex of Escherichia coli adenylate kinase. Proteins 62 2006 555-6 [PubMed: 16302237] http://dx.doi.org/10.1002/prot.20699
	Bellinzoni M, Haouz A, Grana M, Munier-Lehmann H, Shepard W, Alzari PM. The crystal structure of Mycobacterium tuberculosis adenylate kinase in complex with two molecules of ADP and Mg2+ supports an associative mechanism for phosphoryl transfer. Protein Sci. 15 2006 1489-93 [PubMed: 16672241] http://dx.doi.org/10.1110/ps.062163406
	Berry MB, Phillips GN Jr. Crystal structures of Bacillus stearothermophilus adenylate kinase with bound Ap5A, Mg2+ Ap5A, and Mn2+ Ap5A reveal an intermediate lid position and six coordinate octahedral geometry for bound Mg2+ and Mn2+. Proteins 32 1998 276-88 [PubMed: 9715904] http://dx.doi.org/10.1002/(SICI)1097-0134(19980815)32:3<276::AID-PROT3>3.0.CO;2-G
	Counago R, Chen S, Shamoo Y. In vivo molecular evolution reveals biophysical origins of organismal fitness. Mol. Cell 22 2006 441-9 [PubMed: 16713575] http://dx.doi.org/10.1016/j.molcel.2006.04.012
	Henzler-Wildman KA, Thai V, Lei M, Ott M, Wolf-Watz M, Fenn T, Pozharski E, Wilson MA, Petsko GA, Karplus M, Hubner CG, Kern D. Intrinsic motions along an enzymatic reaction trajectory. Nature 450 2007 838-44 [PubMed: 18026086] http://dx.doi.org/10.1038/nature06410

InterPro 23.1