ID   AROK_CERS4              Reviewed;         199 AA.
AC   Q3J2I9;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 2.
DT   03-AUG-2022, entry version 94.
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=RHOS4_14270;
GN   ORFNames=RSP_2817;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) 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; CP000143; ABA78995.2; -; Genomic_DNA.
DR   RefSeq; WP_017140213.1; NZ_CP030271.1.
DR   RefSeq; YP_352896.2; NC_007493.2.
DR   AlphaFoldDB; Q3J2I9; -.
DR   SMR; Q3J2I9; -.
DR   STRING; 272943.RSP_2817; -.
DR   EnsemblBacteria; ABA78995; ABA78995; RSP_2817.
DR   GeneID; 57470156; -.
DR   KEGG; rsp:RSP_2817; -.
DR   PATRIC; fig|272943.9.peg.1765; -.
DR   eggNOG; COG0703; Bacteria.
DR   OMA; IGKHLFE; -.
DR   UniPathway; UPA00053; UER00088.
DR   Proteomes; UP000002703; Chromosome 1.
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..199
FT                   /note="Shikimate kinase"
FT                   /id="PRO_0000237921"
FT   BINDING         34..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT   BINDING         38
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT   BINDING         80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT   BINDING         102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT   BINDING         140
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT   BINDING         159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
SQ   SEQUENCE   199 AA;  22077 MW;  F9BE08DF99A8BD91 CRC64;
     MKVGAEVRRR GNREDGRQVM ARLKKTVVMV GMMGAGKTAV GSALARGLNV PFLDSDEEIE
     RAANRTIAEI FARDGEPFFR EKESQVLARL LRGSPCVLST GGGAFMAEGN RRMIREQGVS
     VWLKADLDVL WHRVRHKATR PLLRTPNPRE TLRALLEARD PVYAQADLAV ESGEGTVEQM
     AVRVREALAT RPDVLETDE