Shikimate kinase 1 - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P0A6D7 (AROK_ECOLI)

Last modified January 19, 2010. Version 51. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Shikimate kinase 1
      Short name=SK 1
    EC=2.7.1.71
Alternative name(s):
    Shikimate kinase I
      Short name=SKI

Gene names

Name:	aroK
Ordered Locus Names:	b3390, JW5947

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	173 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. Ref.1
Catalytic activity	ATP + shikimate = ADP + shikimate 3-phosphate. HAMAP MF_00109
Cofactor	Binds 1 magnesium ion per subunit Probable. HAMAP MF_00109
Pathway	Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. HAMAP MF_00109
Subunit structure	Monomer. Ref.11
Subcellular location	Cytoplasm Probable HAMAP MF_00109.
Induction	Constitutively expressed. HAMAP MF_00109
Domain	The LID domain closes over the active site upon ATP binding. HAMAP MF_00109
Miscellaneous	Two isozymes have been found in E.coli. AroK has 100-fold lower affinity for shikimate than aroL, suggesting that aroL is the dominant enzyme in the biosynthesis of the aromatic amino acids, with aroK playing a secondary role and possibly participating in an as yet unidentified cellular process. HAMAP MF_00109
Sequence similarities	Belongs to the shikimate kinase family.
Biophysicochemical properties	Kinetic parameters: K_M=20 mM for shikimate Ref.10
Sequence caution	The sequence AAC36834.1 differs from that shown. Reason: Frameshift at position 98. The sequence CAA79665.1 differs from that shown. Reason: Frameshift at position 98.

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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 Direct protein sequencing
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...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.8 Ref.9

Chain

2 – 173

172

Shikimate kinase 1 HAMAP MF_00109

PRO_0000192377

Regions

Nucleotide binding

14 – 19

ATP By similarity

Region

116 – 127

Lid domain HAMAP MF_00109

Sites

Metal binding

Magnesium By similarity

Binding site

Substrate By similarity

Binding site

Substrate By similarity

Binding site

Substrate; via amide nitrogen By similarity

Binding site

120

ATP By similarity

Binding site

140

Substrate By similarity

Binding site

157

ATP By similarity

Secondary structure

173

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P0A6D7-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 5681B562B5CD4674
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FASTA

173

19,538

        10         20         30         40         50         60 
MAEKRNIFLV GPMGAGKSTI GRQLAQQLNM EFYDSDQEIE KRTGADVGWV FDLEGEEGFR 

        70         80         90        100        110        120 
DREEKVINEL TEKQGIVLAT GGGSVKSRET RNRLSARGVV VYLETTIEKQ LARTQRDKKR 

       130        140        150        160        170 
PLLHVETPPR EVLEALANER NPLYEEIADV TIRTDDQSAK VVANQIIHML ESN

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of the gene (aroK) encoding shikimic acid kinase I of Escherichia coli." Lobner-Olesen A., Boye E., Marinus M.G. J. Bacteriol. 174:525-529(1992) [PubMed: 1309529] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: K12.
[2]	"Expression of the Escherichia coli dam gene." Lobner-Olesen A., Boye E., Marinus M.G. Mol. Microbiol. 6:1841-1851(1992) [PubMed: 1630320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The gene (aroK) encoding shikimate kinase I from Escherichia coli." Griffin H.G., Gasson M.J. DNA Seq. 5:195-197(1995) [PubMed: 7612934] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[4]	"A reassessment of the relationship between aroK- and aroL-encoded shikimate kinase enzymes of Escherichia coli." Whipp M.J., Pittard A.J. J. Bacteriol. 177:1627-1629(1995) [PubMed: 7883721] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[5]	"Characterization of three genes in the dam-containing operon of Escherichia coli." Lyngstadaas A., Lobner-Olesen A., Boye E. Mol. Gen. Genet. 247:546-554(1995) [PubMed: 7603433] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[7]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2.
[9]	"Protein identification with N and C-terminal sequence tags in proteome projects." Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F. J. Mol. Biol. 278:599-608(1998) [PubMed: 9600841] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-5. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[10]	"Purification and properties of shikimate kinase II from Escherichia coli K-12." DeFeyter R.C., Pittard J. J. Bacteriol. 165:331-333(1986) [PubMed: 3001029] [Abstract] Cited for: KINETIC PARAMETERS. Strain: K12.
[11]	"Crystal structure of the Escherichia coli shikimate kinase I (AroK) that confers sensitivity to mecillinam." Romanowski M.J., Burley S.K. Proteins 47:558-562(2002) [PubMed: 12001235] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS), SUBUNIT.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M76389 Unassigned DNA. Translation: AAC36834.1. Frameshift.
X80167 Genomic DNA. Translation: CAA56448.1.
L39822 Genomic DNA. Translation: AAB59099.1.
Z19601 Genomic DNA. Translation: CAA79665.1. Frameshift.
U18997 Genomic DNA. Translation: AAA58187.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76415.1. Different initiation.
AP009048 Genomic DNA. Translation: BAE77901.1.

PIR

A65134.

RefSeq

AP_004400.1.
YP_026215.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KAG	X-ray	2.05	A/B	1-173	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P0A6D7.

2-D gel databases

SWISS-2DPAGE

P0A6D7.

Genome annotation databases

GeneID

2847759.

GenomeReviews

Gene locus JW5947 in contig AP009048_GR.
Gene locus b3390 in contig U00096_GR.

KEGG

ecj:JW5947.
eco:b3390.

Organism-specific databases

EchoBASE

EB0079.

EcoGene

EG10081. aroK.

CMR

Search...

Phylogenomic databases

eggNOG

COG0703.

HOGENOM

HBG335815.

OMA

HANVFFV.

Enzyme and pathway databases

BioCyc

EcoCyc:AROK-MONOMER.
ECOL168927:B3390-MONOMER.
MetaCyc:AROK-MONOMER.

Gene expression databases

Genevestigator

P0A6D7.

Family and domain databases

HAMAP

MF_00109. Shikimate_kinase.
[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...

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Entry information

Entry name

AROK_ECOLI

Accession

Primary (citable) accession number: P0A6D7
Secondary accession number(s): P24167

Q8X4S0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	January 23, 2007
Last modified:	January 19, 2010
This is version 51 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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

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