AROK_HELPY
ID AROK_HELPY Reviewed; 162 AA.
AC P56073;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Shikimate kinase;
DE Short=SK;
DE EC=2.7.1.71;
GN Name=aroK; OrderedLocusNames=HP_0157;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP INHIBITORS.
RX PubMed=17098431; DOI=10.1016/j.bmc.2006.10.058;
RA Han C., Zhang J., Chen L., Chen K., Shen X., Jiang H.;
RT "Discovery of Helicobacter pylori shikimate kinase inhibitors: bioassay and
RT molecular modeling.";
RL Bioorg. Med. Chem. 15:656-662(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF APOENYZME AND IN COMPLEX WITH
RP SHIKIMATE, FUNCTION, CATALYTIC ACTIVITY, AND KINETIC PARAMETERS.
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=16291688; DOI=10.1128/jb.187.23.8156-8163.2005;
RA Cheng W.-C., Chang Y.-N., Wang W.-C.;
RT "Structural basis for shikimate-binding specificity of Helicobacter pylori
RT shikimate kinase.";
RL J. Bacteriol. 187:8156-8163(2005).
CC -!- FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl
CC group of shikimic acid using ATP as a cosubstrate.
CC {ECO:0000269|PubMed:16291688}.
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; Evidence={ECO:0000269|PubMed:16291688};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=60 uM for shikimate {ECO:0000269|PubMed:16291688};
CC KM=101 uM for MgATP {ECO:0000269|PubMed:16291688};
CC Vmax=22 umol/min/mg enzyme toward shikimate
CC {ECO:0000269|PubMed:16291688};
CC Vmax=26 umol/min/mg enzyme toward MgATP
CC {ECO:0000269|PubMed:16291688};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 5/7.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the shikimate kinase family. {ECO:0000305}.
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DR EMBL; AE000511; AAD07220.1; -; Genomic_DNA.
DR PIR; E64539; E64539.
DR RefSeq; NP_206956.1; NC_000915.1.
DR RefSeq; WP_001164290.1; NC_018939.1.
DR PDB; 1ZUH; X-ray; 1.80 A; A=1-162.
DR PDB; 1ZUI; X-ray; 2.30 A; A=1-162.
DR PDB; 3HR7; X-ray; 1.80 A; A/B=1-162.
DR PDB; 3MRS; X-ray; 2.40 A; A=1-162.
DR PDB; 3MUF; X-ray; 2.30 A; A=1-162.
DR PDB; 3N2E; X-ray; 2.53 A; A/B/C=1-162.
DR PDBsum; 1ZUH; -.
DR PDBsum; 1ZUI; -.
DR PDBsum; 3HR7; -.
DR PDBsum; 3MRS; -.
DR PDBsum; 3MUF; -.
DR PDBsum; 3N2E; -.
DR AlphaFoldDB; P56073; -.
DR SMR; P56073; -.
DR STRING; 85962.C694_00785; -.
DR BindingDB; P56073; -.
DR ChEMBL; CHEMBL1075089; -.
DR PaxDb; P56073; -.
DR EnsemblBacteria; AAD07220; AAD07220; HP_0157.
DR KEGG; hpy:HP_0157; -.
DR PATRIC; fig|85962.47.peg.170; -.
DR eggNOG; COG0703; Bacteria.
DR OMA; IGKHLFE; -.
DR PhylomeDB; P56073; -.
DR BRENDA; 2.7.1.71; 2604.
DR SABIO-RK; P56073; -.
DR UniPathway; UPA00053; UER00088.
DR EvolutionaryTrace; P56073; -.
DR PRO; PR:P56073; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
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 InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR031322; Shikimate/glucono_kinase.
DR InterPro; IPR000623; Shikimate_kinase/TSH1.
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; Reference proteome; Transferase.
FT CHAIN 1..162
FT /note="Shikimate kinase"
FT /id="PRO_0000192387"
FT REGION 109..123
FT /note="LID domain"
FT BINDING 11..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 15
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="substrate"
FT BINDING 57
FT /ligand="substrate"
FT BINDING 80
FT /ligand="substrate"
FT BINDING 116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="substrate"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1ZUH"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:1ZUH"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1ZUH"
FT HELIX 32..40
FT /evidence="ECO:0007829|PDB:1ZUH"
FT HELIX 44..50
FT /evidence="ECO:0007829|PDB:1ZUH"
FT HELIX 53..68
FT /evidence="ECO:0007829|PDB:1ZUH"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1ZUH"
FT HELIX 80..84
FT /evidence="ECO:0007829|PDB:1ZUH"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1ZUH"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:1ZUH"
FT HELIX 101..108
FT /evidence="ECO:0007829|PDB:1ZUH"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:3MUF"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:1ZUI"
FT HELIX 123..138
FT /evidence="ECO:0007829|PDB:1ZUH"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:1ZUH"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:1ZUH"
FT HELIX 150..159
FT /evidence="ECO:0007829|PDB:1ZUH"
SQ SEQUENCE 162 AA; 18411 MW; 3D4B5F74E1C958FE CRC64;
MQHLVLIGFM GSGKSSLAQE LGLALKLEVL DTDMIISERV GLSVREIFEE LGEDNFRMFE
KNLIDELKTL KTPHVISTGG GIVMHENLKG LGTTFYLKMD FETLIKRLNQ KEREKRPLLN
NLTQAKELFE KRQALYEKNA SFIIDARGGL NNSLKQVLQF IA
