ID   AROK_SHEPA              Reviewed;         171 AA.
AC   A8GZ29;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Spea_0238;
OS   Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=398579;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700345 / ANG-SQ1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S.Z., Manno D., Hawari J., Richardson P.;
RT   "Complete sequence of Shewanella pealeana ATCC 700345.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000851; ABV85566.1; -; Genomic_DNA.
DR   RefSeq; WP_012153507.1; NC_009901.1.
DR   AlphaFoldDB; A8GZ29; -.
DR   SMR; A8GZ29; -.
DR   STRING; 398579.Spea_0238; -.
DR   EnsemblBacteria; ABV85566; ABV85566; Spea_0238.
DR   KEGG; spl:Spea_0238; -.
DR   eggNOG; COG0703; Bacteria.
DR   HOGENOM; CLU_057607_2_2_6; -.
DR   OMA; IGKHLFE; -.
DR   UniPathway; UPA00053; UER00088.
DR   Proteomes; UP000002608; Chromosome.
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   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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; ATP-binding;
KW   Cytoplasm; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..171
FT                   /note="Shikimate kinase"
FT                   /id="PRO_1000075958"
FT   BINDING         14..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT   BINDING         18
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT   BINDING         36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT   BINDING         60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT   BINDING         82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT   BINDING         120
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT   BINDING         156
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
SQ   SEQUENCE   171 AA;  19113 MW;  14F0460D8234264D CRC64;
     MAEKRNIFLV GPMGAGKSTI GRHLAQMLHL EFHDSDQEIE SRTGADIAWV FDVEGEEGFR
     IRETQVVADL TEKQGIVLAT GGGSIQSKEI RNNLSARGIV VYLETTIDKQ VARTQRDKRR
     PLLQVDDPRE VLESLAEVRN PLYEEIADVI VKTDEQSAKV VANQIIEQLG F