Shikimate kinase 2 - Erwinia chrysanthemi

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P10880 (AROL_ERWCH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 81. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Shikimate kinase 2
Short name=SK 2
EC=2.7.1.71

Alternative name(s):
Shikimate kinase II
Short name=SKII

Gene names

Name:	aroL
Synonyms:	aroM

Organism

Erwinia chrysanthemi

Taxonomic identifier

556 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Dickeya

Protein attributes

Sequence length	173 AA.
Sequence status	Complete.
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.5
Catalytic activity	ATP + shikimate = ADP + shikimate 3-phosphate. HAMAP MF_01269
Cofactor	Binds 1 magnesium ion per subunit. Ref.4
Enzyme regulation	Inhibited by chloride and sulfate ions. Ref.3
Pathway	Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. HAMAP MF_01269
Subunit structure	Monomer. Ref.2
Subcellular location	Cytoplasm By similarity HAMAP MF_01269.
Domain	The LID domain closes over the active site upon ATP binding. HAMAP MF_01269
Sequence similarities	Belongs to the shikimate kinase family. AroL subfamily.
Caution	It is uncertain whether the initial Met is cleaved or not.
Biophysicochemical properties	Kinetic parameters: K_M=310 µM for shikimate Ref.5 K_M=620 µM for ATP
Mass spectrometry	Molecular mass is 18955 Da from positions 1 - 173. Determined by ESI. Ref.2 Molecular mass is 18824 Da from positions 2 - 173. Determined by ESI. Ref.2

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
Gene Ontology (GO)
Biological process	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW shikimate kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 173

173

Shikimate kinase 2 HAMAP MF_01269

PRO_0000192383

Regions

Nucleotide binding

12 – 17

ATP HAMAP MF_01269

Region

112 – 126

LID domain HAMAP MF_01269

Sites

Metal binding

Magnesium

Metal binding

Magnesium

Binding site

Substrate Probable

Binding site

Substrate Probable

Binding site

Substrate; via amide nitrogen By similarity

Binding site

120

ATP By similarity

Binding site

139

Substrate Probable

Binding site

155

ATP

Experimental info

Mutagenesis

C → S: 66% of wild-type activity. Increase in substrates affinity. Ref.5

Mutagenesis

K → M: Loss of activity. Increased thermostability. Ref.5

Mutagenesis

D → N: Loss of activity. Ref.5

Mutagenesis

162

C → S: No effect on activity and substrates affinity. Ref.5

Secondary structure

173

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P10880 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: AE28692D0B25B577
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FASTA

173

18,956

        10         20         30         40         50         60 
MTEPIFMVGA RGCGKTTVGR ELARALGYEF VDTDIFMQHT SGMTVADVVA AEGWPGFRRR 

        70         80         90        100        110        120 
ESEALQAVAT PNRVVATGGG MVLLEQNRQF MRAHGTVVYL FAPAEELALR LQASPQAHQR 

       130        140        150        160        170 
PTLTGRPIAE EMEAVLRERE ALYQDVAHYV VDATQPPAAI VCELMQTMRL PAA

« Hide

References

[1]	"Nucleotide sequence of an Erwinia chrysanthemi gene encoding shikimate kinase." Minton N.P., Whitehead P.J., Atkinson T., Gilbert H.J. Nucleic Acids Res. 17:1769-1769(1989) [PubMed: 2537963] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Crystallization and preliminary X-ray crystallographic analysis of shikimate kinase from Erwinia chrysanthemi." Krell T., Coyle J.E., Horsburgh M.J., Coggins J.R., Lapthorn A.J. Acta Crystallogr. D 53:612-614(1997) [PubMed: 15299895] [Abstract] Cited for: CRYSTALLIZATION, MASS SPECTROMETRY, SUBUNIT.
[3]	"Effects of salts on the function and conformational stability of shikimate kinase." Cerasoli E., Kelly S.M., Coggins J.R., Lapthorn A.J., Clarke D.T., Price N.C. Biochim. Biophys. Acta 1648:43-54(2003) [PubMed: 12758146] [Abstract] Cited for: ENZYME REGULATION, EFFECTS OF SALTS.
[4]	"The three-dimensional structure of shikimate kinase." Krell T., Coggins J.R., Lapthorn A.J. J. Mol. Biol. 278:983-997(1998) [PubMed: 9600856] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX WITH MG-ADP, COFACTOR. Strain: NCPPB 1066.
[5]	"Biochemical and X-ray crystallographic studies on shikimate kinase: the important structural role of the P-loop lysine." Krell T., Maclean J., Boam D.J., Cooper A., Resmini M., Brocklehurst K., Kelly S.M., Price N.C., Lapthorn A.J., Coggins J.R. Protein Sci. 10:1137-1149(2001) [PubMed: 11369852] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT MET-15, FUNCTION, KINETIC PARAMETERS, MUTAGENESIS OF CYS-13; LYS-15; ASP-34 AND CYS-162.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X14777 Genomic DNA. Translation: CAA32883.1.

PIR

S09613.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E6C	X-ray	1.80	A/B	1-173	[»]
1SHK	X-ray	1.90	A/B	1-173	[»]
2SHK	X-ray	2.60	A/B	1-173	[»]

ProteinModelPortal

P10880.

SMR

P10880. Positions 1-170.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

HAMAP

MF_01269. Shikimate_kinase_2.
[Tree]

InterPro

IPR000623. Shikimate_kinase.
IPR023000. Shikimate_kinase_CS.
[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

AROL_ERWCH

Accession

Primary (citable) accession number: P10880

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	May 31, 2011
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents