AROK_COXBU
ID AROK_COXBU Reviewed; 179 AA.
AC Q83AJ3;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Shikimate kinase {ECO:0000255|HAMAP-Rule:MF_00109};
DE Short=SK {ECO:0000255|HAMAP-Rule:MF_00109};
DE EC=2.7.1.71 {ECO:0000255|HAMAP-Rule:MF_00109};
GN Name=aroK {ECO:0000255|HAMAP-Rule:MF_00109}; OrderedLocusNames=CBU_1892;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
CC -!- FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl
CC group of shikimic acid using ATP as a cosubstrate. {ECO:0000255|HAMAP-
CC Rule:MF_00109}.
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:0000255|HAMAP-Rule:MF_00109};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00109};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00109};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 5/7. {ECO:0000255|HAMAP-Rule:MF_00109}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00109}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00109}.
CC -!- SIMILARITY: Belongs to the shikimate kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00109}.
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DR EMBL; AE016828; AAO91383.1; -; Genomic_DNA.
DR RefSeq; NP_820869.1; NC_002971.3.
DR RefSeq; WP_010958519.1; NZ_CCYB01000008.1.
DR PDB; 3TRF; X-ray; 2.60 A; A/B=1-179.
DR PDBsum; 3TRF; -.
DR AlphaFoldDB; Q83AJ3; -.
DR SMR; Q83AJ3; -.
DR STRING; 227377.CBU_1892; -.
DR EnsemblBacteria; AAO91383; AAO91383; CBU_1892.
DR GeneID; 1209805; -.
DR KEGG; cbu:CBU_1892; -.
DR PATRIC; fig|227377.7.peg.1875; -.
DR eggNOG; COG0703; Bacteria.
DR HOGENOM; CLU_057607_2_2_6; -.
DR OMA; IGKHLFE; -.
DR UniPathway; UPA00053; UER00088.
DR EvolutionaryTrace; Q83AJ3; -.
DR Proteomes; UP000002671; 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..179
FT /note="Shikimate kinase"
FT /id="PRO_0000237869"
FT BINDING 15..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT BINDING 19
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT BINDING 37
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT BINDING 61
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:3TRF"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:3TRF"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:3TRF"
FT HELIX 36..44
FT /evidence="ECO:0007829|PDB:3TRF"
FT HELIX 48..73
FT /evidence="ECO:0007829|PDB:3TRF"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:3TRF"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:3TRF"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:3TRF"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:3TRF"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:3TRF"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:3TRF"
FT HELIX 129..149
FT /evidence="ECO:0007829|PDB:3TRF"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:3TRF"
FT HELIX 161..171
FT /evidence="ECO:0007829|PDB:3TRF"
SQ SEQUENCE 179 AA; 20335 MW; A47C31B7EF35941C CRC64;
MKKNLTNIYL IGLMGAGKTS VGSQLAKLTK RILYDSDKEI EKRTGADIAW IFEMEGEAGF
RRREREMIEA LCKLDNIILA TGGGVVLDEK NRQQISETGV VIYLTASIDT QLKRIGQKGE
MRRPLFIKNN SKEKLQQLNE IRKPLYQAMA DLVYPTDDLN PRQLATQILV DIKQTYSDL
