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InterPro: IPR000623 Shikimate kinase

Protein matches Help

UniProtKB

Matches:

3099 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

IPR000623 Shik_kinase

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01202	SKI	3034
PRINTS	PR01100	SHIKIMTKNASE	2111
PROSITE pattern	PS01128	SHIKIMATE_KINASE	1401
Signatures in BioMart

InterPro Relationships Help

Found in

IPR008289 Pentafunctional AroM protein

GO Term annotation Help

Function

GO:0004765 shikimate kinase activity
GO:0005524 ATP binding

InterPro annotation

Entry Details in BioMart

Abstract

Shikimate kinase (EC:2.7.1.71) catalyses the fifth step in the biosynthesis of aromatic amino acids from chorismate (the so-called shikimate pathway) [1]. The enzyme catalyses the following reaction:

ATP + shikimate = ADP + shikimate-3-phosphate

The protein is found in bacteria (gene aroK or aroL), plants and fungi (where it is part of a multifunctional enzyme that catalyses five consecutive steps in this pathway). In 1994, the 3D structure of shikimate kinase was predicted to be very close to that of adenylate kinase, suggesting a functional similarity as well as an evolutionary relationship [2]. This prediction has since been confirmed experimentally. The protein is reported to possess an alpha/beta fold, consisting of a central sheet of five parallel beta-strands flanked by alpha-helices. Such a topology is very similar to that of adenylate kinase [3].

Structural links Help

PDB - click here

SCOP: c.37.1.17 , c.37.1.2

CATH: 3.40.50.300

Database links Help

PDBe-motif: PS01128

Enzyme: EC:2.7.1.71

PROSITE doc: PDOC00868

PANDIT: PF01202

Blocks: IPB000623

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

IPR000623

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P08566 Pentafunctional AROM polypeptide

Q09527 Probable adenylate kinase isoenzyme 6

Q5T6J7 Probable gluconokinase

Q8BH55 Threonine synthase-like 1

Q9SJ05 Shikimate kinase, chloroplastic

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013785	Aldolase-type TIM barrel
IPR013792	RNA 3'-terminal phosphate cyclase/enolpyruvate transferase, alpha/beta
IPR003959	ATPase, AAA-type, core
IPR002658	3-dehydroquinate synthase AroB
IPR013708	Shikimate dehydrogenase substrate binding, N-terminal
IPR010110	Shikimate-5-dehydrogenase
IPR008289	Pentafunctional AroM protein
IPR016037	3-dehydroquinate synthase AroB, subgroup
IPR006001	Carbohydrate kinase, thermoresistant glucokinase
IPR004450	Threonine synthase
IPR000623	Shikimate kinase
IPR001381	Dehydroquinase class I
IPR018508	3-dehydroquinate dehydratase, active site
IPR016040	NAD(P)-binding domain
IPR001926	Pyridoxal phosphate-dependent enzyme, beta subunit
IPR006151	Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase
IPR006264	3-phosphoshikimate 1-carboxyvinyltransferase, subgroup
IPR001986	3-phosphoshikimate 1-carboxyvinyltransferase, core
	ModBase
	SWISS-MODEL

Publications Open in usermanual
1.	Griffin HG, Gasson MJ. The gene (aroK) encoding shikimate kinase I from Escherichia coli. DNA Seq. 5 195-7 1995 [PubMed: 7612934]
2.	Matsuo Y, Nishikawa K. Protein structural similarities predicted by a sequence-structure compatibility method. Protein Sci. 3 2055-63 1994 [PubMed: 7703851] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=7703851
3.	Krell T, Coggins JR, Lapthorn AJ. The three-dimensional structure of shikimate kinase. J. Mol. Biol. 278 983-97 1998 [PubMed: 9600856] http://dx.doi.org/10.1006/jmbi.1998.1755

Additional Reading Open in usermanual
	Hartmann MD, Bourenkov GP, Oberschall A, Strizhov N, Bartunik HD. Mechanism of phosphoryl transfer catalyzed by shikimate kinase from Mycobacterium tuberculosis. J. Mol. Biol. 364 2006 411-23 [PubMed: 17020768] http://dx.doi.org/10.1016/j.jmb.2006.09.001
	Pereira JH, de Oliveira JS, Canduri F, Dias MV, Palma MS, Basso LA, Santos DS, de Azevedo WF Jr. Structure of shikimate kinase from Mycobacterium tuberculosis reveals the binding of shikimic acid. Acta Crystallogr. D Biol. Crystallogr. 60 2004 2310-9 [PubMed: 15583379] http://dx.doi.org/10.1107/S090744490402517X
	Gan J, Gu Y, Li Y, Yan H, Ji X. Crystal structure of Mycobacterium tuberculosis shikimate kinase in complex with shikimic acid and an ATP analogue. Biochemistry 45 2006 8539-45 [PubMed: 16834327] http://dx.doi.org/10.1021/bi0606290
	Dhaliwal B, Nichols CE, Ren J, Lockyer M, Charles I, Hawkins AR, Stammers DK. Crystallographic studies of shikimate binding and induced conformational changes in Mycobacterium tuberculosis shikimate kinase. FEBS Lett. 574 2004 49-54 [PubMed: 15358538] http://dx.doi.org/10.1016/j.febslet.2004.08.005
	Dias MV, Faim LM, Vasconcelos IB, de Oliveira JS, Basso LA, Santos DS, de Azevedo WF Jr. Effects of the magnesium and chloride ions and shikimate on the structure of shikimate kinase from Mycobacterium tuberculosis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 2007 1-6 [PubMed: 17183161]

InterPro 23.1