AROL_DICCH
ID AROL_DICCH Reviewed; 173 AA.
AC P10880;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Shikimate kinase 2;
DE Short=SK 2;
DE EC=2.7.1.71;
DE AltName: Full=Shikimate kinase II;
DE Short=SKII;
GN Name=aroL; Synonyms=aroM;
OS Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=556;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2537963; DOI=10.1093/nar/17.4.1769;
RA Minton N.P., Whitehead P.J., Atkinson T., Gilbert H.J.;
RT "Nucleotide sequence of an Erwinia chrysanthemi gene encoding shikimate
RT kinase.";
RL Nucleic Acids Res. 17:1769-1769(1989).
RN [2]
RP CRYSTALLIZATION, MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=15299895; DOI=10.1107/s0907444997004319;
RA Krell T., Coyle J.E., Horsburgh M.J., Coggins J.R., Lapthorn A.J.;
RT "Crystallization and preliminary X-ray crystallographic analysis of
RT shikimate kinase from Erwinia chrysanthemi.";
RL Acta Crystallogr. D 53:612-614(1997).
RN [3]
RP ACTIVITY REGULATION, AND EFFECTS OF SALTS.
RX PubMed=12758146; DOI=10.1016/s1570-9639(03)00110-9;
RA Cerasoli E., Kelly S.M., Coggins J.R., Lapthorn A.J., Clarke D.T.,
RA Price N.C.;
RT "Effects of salts on the function and conformational stability of shikimate
RT kinase.";
RL Biochim. Biophys. Acta 1648:43-54(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX WITH
RP MG-ADP, AND COFACTOR.
RC STRAIN=NCPPB 1066;
RX PubMed=9600856; DOI=10.1006/jmbi.1998.1755;
RA Krell T., Coggins J.R., Lapthorn A.J.;
RT "The three-dimensional structure of shikimate kinase.";
RL J. Mol. Biol. 278:983-997(1998).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT MET-15, FUNCTION, KINETIC
RP PARAMETERS, AND MUTAGENESIS OF CYS-13; LYS-15; ASP-34 AND CYS-162.
RX PubMed=11369852; DOI=10.1110/ps.52501;
RA Krell T., Maclean J., Boam D.J., Cooper A., Resmini M., Brocklehurst K.,
RA Kelly S.M., Price N.C., Lapthorn A.J., Coggins J.R.;
RT "Biochemical and X-ray crystallographic studies on shikimate kinase: the
RT important structural role of the P-loop lysine.";
RL Protein Sci. 10:1137-1149(2001).
CC -!- FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl
CC group of shikimic acid using ATP as a cosubstrate.
CC {ECO:0000269|PubMed:11369852}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+);
CC Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216;
CC EC=2.7.1.71;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9600856};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:9600856};
CC -!- ACTIVITY REGULATION: Inhibited by chloride and sulfate ions.
CC {ECO:0000269|PubMed:12758146}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=310 uM for shikimate {ECO:0000269|PubMed:11369852};
CC KM=620 uM for ATP {ECO:0000269|PubMed:11369852};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 5/7.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15299895}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The LID domain closes over the active site upon ATP binding.
CC -!- MASS SPECTROMETRY: Mass=18955; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15299895};
CC -!- SIMILARITY: Belongs to the shikimate kinase family. AroL subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether the initial Met is cleaved or not.
CC {ECO:0000305}.
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DR EMBL; X14777; CAA32883.1; -; Genomic_DNA.
DR PIR; S09613; S09613.
DR PDB; 1E6C; X-ray; 1.80 A; A/B=1-173.
DR PDB; 1SHK; X-ray; 1.90 A; A/B=1-173.
DR PDB; 2SHK; X-ray; 2.60 A; A/B=1-173.
DR PDBsum; 1E6C; -.
DR PDBsum; 1SHK; -.
DR PDBsum; 2SHK; -.
DR AlphaFoldDB; P10880; -.
DR SMR; P10880; -.
DR SABIO-RK; P10880; -.
DR UniPathway; UPA00053; UER00088.
DR EvolutionaryTrace; P10880; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00464; SK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00109; Shikimate_kinase; 1.
DR HAMAP; MF_01269; Shikimate_kinase_2; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR031322; Shikimate/glucono_kinase.
DR InterPro; IPR000623; Shikimate_kinase/TSH1.
DR InterPro; IPR027544; Shikimate_kinase_2.
DR InterPro; IPR023000; Shikimate_kinase_CS.
DR Pfam; PF01202; SKI; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS01128; SHIKIMATE_KINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..173
FT /note="Shikimate kinase 2"
FT /id="PRO_0000192383"
FT REGION 112..126
FT /note="LID domain"
FT BINDING 12..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 16
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 32
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 34
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MUTAGEN 13
FT /note="C->S: 66% of wild-type activity. Increase in
FT substrates affinity."
FT /evidence="ECO:0000269|PubMed:11369852"
FT MUTAGEN 15
FT /note="K->M: Loss of activity. Increased thermostability."
FT /evidence="ECO:0000269|PubMed:11369852"
FT MUTAGEN 34
FT /note="D->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11369852"
FT MUTAGEN 162
FT /note="C->S: No effect on activity and substrates
FT affinity."
FT /evidence="ECO:0000269|PubMed:11369852"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:1E6C"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:1E6C"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:1E6C"
FT HELIX 33..41
FT /evidence="ECO:0007829|PDB:1E6C"
FT HELIX 45..68
FT /evidence="ECO:0007829|PDB:1E6C"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:1E6C"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1E6C"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:1E6C"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:1E6C"
FT HELIX 104..115
FT /evidence="ECO:0007829|PDB:1E6C"
FT HELIX 125..146
FT /evidence="ECO:0007829|PDB:1E6C"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:1E6C"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:1E6C"
SQ SEQUENCE 173 AA; 18956 MW; AE28692D0B25B577 CRC64;
MTEPIFMVGA RGCGKTTVGR ELARALGYEF VDTDIFMQHT SGMTVADVVA AEGWPGFRRR
ESEALQAVAT PNRVVATGGG MVLLEQNRQF MRAHGTVVYL FAPAEELALR LQASPQAHQR
PTLTGRPIAE EMEAVLRERE ALYQDVAHYV VDATQPPAAI VCELMQTMRL PAA
