Reviewed, UniProtKB/Swiss-Prot P0A4Z2 (AROK_MYCTU)

Names and origin

Protein names

Recommended name:
    Shikimate kinase
      Short name=SK
    EC=2.7.1.71

Gene names

Name:	aroK
Ordered Locus Names:	Rv2539c, MT2614
ORF Names:	MTCY159.17

Organism

Mycobacterium tuberculosis [Complete proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	176 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. Ref.1 Ref.9
Catalytic activity	ATP + shikimate = ADP + shikimate 3-phosphate. HAMAP MF_00109
Cofactor	Binds 1 magnesium ion per subunit. Ref.5 Ref.6
Pathway	Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. HAMAP MF_00109
Subunit structure	Monomer. Ref.1
Subcellular location	Cytoplasm Probable.
Domain	Consists of three domains: the CORE domain which forms the binding site for nucleotides, the LID domain which closes over the active site upon ATP or shikimate binding, and the substrate-binding domain which functions to recognize and bind shikimate. HAMAP MF_00109
Miscellaneous	The phosphoryl transfer proceeds by an in-line associative mechanism. The random sequential binding of shikimate and nucleotide is associated with domain movements that suggest a synergic mechanism by which binding of the first substrate may enhance the affinity for the second substrate. HAMAP MF_00109
Sequence similarities	Belongs to the shikimate kinase family.
Biophysicochemical properties	Kinetic parameters: KM=410 µM for shikimate Ref.5 KM=83 µM for ATP

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP shikimate kinase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 176

176

Shikimate kinase HAMAP MF_00109

PRO_0000192393

Regions

Nucleotide binding

12 – 17

6

ATP HAMAP MF_00109

Region

112 – 124

13

LID domain HAMAP MF_00109

Sites

Metal binding

16

1

Magnesium HAMAP MF_00109

Binding site

34

1

Substrate HAMAP MF_00109

Binding site

58

1

Substrate HAMAP MF_00109

Binding site

80

1

Substrate; via amide nitrogen HAMAP MF_00109

Binding site

117

1

ATP HAMAP MF_00109

Binding site

136

1

Substrate HAMAP MF_00109

Binding site

153

1

ATP HAMAP MF_00109

Secondary structure

1

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176

Helix Strand Turn

Details...

Beta strand

4 – 8

5

Helix

15 – 26

12

Beta strand

30 – 32

3

Helix

33 – 41

9

Helix

45 – 52

8

Helix

54 – 71

18

Beta strand

74 – 77

4

Helix

82 – 84

3

Helix

86 – 92

7

Beta strand

97 – 101

5

Helix

104 – 110

7

Helix

118 – 121

4

Helix

124 – 143

20

Beta strand

145 – 149

5

Helix

155 – 163

9

Turn

173 – 175

3

Sequences

	Sequence		Length	Mass (Da)
	P0A4Z2-1 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 208EE0C38F5186A1	FASTA	176	18,583
	10 20 30 40 50 60 MAPKAVLVGL PGSGKSTIGR RLAKALGVGL LDTDVAIEQR TGRSIADIFA TDGEQEFRRI 70 80 90 100 110 120 EEDVVRAALA DHDGVLSLGG GAVTSPGVRA ALAGHTVVYL EISAAEGVRR TGGNTVRPLL 130 140 150 160 170 AGPDRAEKYR ALMAKRAPLY RRVATMRVDT NRRNPGAVVR HILSRLQVPS PSEAAT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and overexpression in soluble form of functional shikimate kinase and 5-enolpyruvylshikimate 3-phosphate synthase enzymes from Mycobacterium tuberculosis." Oliveira J.S., Pinto C.A., Basso L.A., Santos D.S. Protein Expr. Purif. 22:430-435(2001) [PubMed: 11483005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT.
[2]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[3]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[4]	"Crystallization and preliminary X-ray diffraction analysis of shikimate kinase from Mycobacterium tuberculosis in complex with MgADP." Gu Y., Reshetnikova L., Li Y., Yan H., Singh S.V., Ji X. Acta Crystallogr. D 57:1870-1871(2001) [PubMed: 11717501] [Abstract] Cited for: CRYSTALLIZATION. Strain: ATCC 25618 / H37Rv.
[5]	"Crystal structure of shikimate kinase from Mycobacterium tuberculosis reveals the dynamic role of the LID domain in catalysis." Gu Y., Reshetnikova L., Li Y., Wu Y., Yan H., Singh S.V., Ji X. J. Mol. Biol. 319:779-789(2002) [PubMed: 12054870] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH MG-ADP, COFACTOR, KINETIC PARAMETERS. Strain: ATCC 25618 / H37Rv.
[6]	"Structure of shikimate kinase from Mycobacterium tuberculosis reveals the binding of shikimic acid." Pereira J.H., de Oliveira J.S., Canduri F., Dias M.V.B., Palma M.S., Basso L.A., Santos D.S., de Azevedo W.F. Jr. Acta Crystallogr. D 60:2310-2319(2004) [PubMed: 15583379] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH SHIKIMATE AND MG-ADP, COFACTOR.
[7]	"Crystallographic studies of shikimate binding and induced conformational changes in Mycobacterium tuberculosis shikimate kinase." Dhaliwal B., Nichols C.E., Ren J., Lockyer M., Charles I.G., Hawkins A.R., Stammers D.K. FEBS Lett. 574:49-54(2004) [PubMed: 15358538] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH SHIKIMATE AND ADP.
[8]	"Crystal structure of Mycobacterium tuberculosis shikimate kinase in complex with shikimic acid and an ATP analogue." Gan J., Gu Y., Li Y., Yan H., Ji X. Biochemistry 45:8539-8545(2006) [PubMed: 16834327] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH SUBSTRATES. Strain: ATCC 25618 / H37Rv.
[9]	"Mechanism of phosphoryl transfer catalyzed by shikimate kinase from Mycobacterium tuberculosis." Hartmann M.D., Bourenkov G.P., Oberschall A., Strizhov N., Bartunik H.D. J. Mol. Biol. 364:411-423(2006) [PubMed: 17020768] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH SUBSTRATES AND PRODUCTS, FUNCTION, REACTION MECHANISM. Strain: ATCC 25618 / H37Rv.
[10]	"Effects of the magnesium and chloride ions and shikimate on the structure of shikimate kinase from Mycobacterium tuberculosis." Dias M.V.B., Faim L.M., Vasconcelos I.B., de Oliveira J.S., Basso L.A., Santos D.S., de Azevedo W.F. Jr. Acta Crystallogr. F 63:1-6(2007) [PubMed: 17183161] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH SHIKIMATE AND MG-ADP.

Cross-references

Sequence databases

EMBLGenBankDDBJ

BX842580 Genomic DNA. Translation: CAB06199.1.
AE000516 Genomic DNA. Translation: AAK46924.1.

PIR

G70658.

RefSeq

NP_217055.1.
NP_337110.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1L4U	X-ray	1.80	A	1-176	[»]
1L4Y	X-ray	2.00	A	1-176	[»]
1U8A	X-ray	2.15	A	1-176	[»]
1WE2	X-ray	2.30	A	1-176	[»]
1ZYU	X-ray	2.90	A	1-176	[»]
2DFN	X-ray	1.93	A	1-176	[»]
2DFT	X-ray	2.80	A/B/C/D	1-176	[»]
2G1J	X-ray	2.00	A/B	1-176	[»]
2G1K	X-ray	1.75	A	1-176	[»]
2IYQ	X-ray	1.80	A	1-176	[»]
2IYR	X-ray	1.98	A/B	1-176	[»]
2IYS	X-ray	1.40	A	1-176	[»]
2IYT	X-ray	1.47	A	1-176	[»]
2IYU	X-ray	1.85	A	1-176	[»]
2IYV	X-ray	1.35	A	1-176	[»]
2IYW	X-ray	1.85	A	1-176	[»]
2IYX	X-ray	1.49	A	1-176	[»]
2IYY	X-ray	1.62	A	1-176	[»]
2IYZ	X-ray	2.30	A	1-176	[»]
3BAF	X-ray	2.25	A	1-176	[»]

ModBase

Search...

Genome annotation databases

GeneID

887434.
925704.

GenomeReviews

Gene locus MT2614 in contig AE000516_GR.
Gene locus Rv2539c in contig AL123456_GR.

KEGG

mtc:MT2614.
mtu:Rv2539c.

TIGR

MT2614.

Organism-specific databases

TubercuList

Rv2539c.

Phylogenomic databases

HOGENOM

P0A4Z2.

OMA

HANVFFV.

Enzyme and pathway databases

BRENDA

2.7.1.71. 809.

Family and domain databases

HAMAP

MF_00109.
[Tree]

InterPro

IPR000623. Shik_kinase.
[Graphical view]

Pfam

PF01202. SKI. 1 hit.
[Graphical view]

PRINTS

PR01100. SHIKIMTKNASE.

PROSITE

PS01128. SHIKIMATE_KINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

AROK_MYCTU

Accession

Primary (citable) accession number: P0A4Z2
Secondary accession number(s): P95014

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	November 3, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)