AROK_AQUAE
ID AROK_AQUAE Reviewed; 168 AA.
AC O67925;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=aq_2177;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of shikimate kinase (aq_2177) from Aquifex aeolicus
RT VF5.";
RL Submitted (MAY-2008) to the PDB data bank.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000657; AAC07875.1; -; Genomic_DNA.
DR PIR; A70487; A70487.
DR RefSeq; NP_214494.1; NC_000918.1.
DR RefSeq; WP_010881430.1; NC_000918.1.
DR PDB; 2PT5; X-ray; 2.10 A; A/B/C/D=1-168.
DR PDBsum; 2PT5; -.
DR AlphaFoldDB; O67925; -.
DR SMR; O67925; -.
DR STRING; 224324.aq_2177; -.
DR EnsemblBacteria; AAC07875; AAC07875; aq_2177.
DR KEGG; aae:aq_2177; -.
DR PATRIC; fig|224324.8.peg.1683; -.
DR eggNOG; COG0703; Bacteria.
DR HOGENOM; CLU_057607_4_0_0; -.
DR InParanoid; O67925; -.
DR OMA; IGKHLFE; -.
DR OrthoDB; 1392851at2; -.
DR UniPathway; UPA00053; UER00088.
DR EvolutionaryTrace; O67925; -.
DR Proteomes; UP000000798; 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..168
FT /note="Shikimate kinase"
FT /id="PRO_0000192366"
FT BINDING 10..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT BINDING 116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2PT5"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:2PT5"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:2PT5"
FT HELIX 31..39
FT /evidence="ECO:0007829|PDB:2PT5"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:2PT5"
FT HELIX 52..66
FT /evidence="ECO:0007829|PDB:2PT5"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:2PT5"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:2PT5"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:2PT5"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:2PT5"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:2PT5"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:2PT5"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2PT5"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:2PT5"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:2PT5"
FT HELIX 150..162
FT /evidence="ECO:0007829|PDB:2PT5"
SQ SEQUENCE 168 AA; 19080 MW; AB1500BC484DEDB6 CRC64;
MRIYLIGFMC SGKSTVGSLL SRSLNIPFYD VDEEVQKREG LSIPQIFEKK GEAYFRKLEF
EVLKDLSEKE NVVISTGGGL GANEEALNFM KSRGTTVFID IPFEVFLERC KDSKERPLLK
RPLDEIKNLF EERRKIYSKA DIKVKGEKPP EEVVKEILLS LEGNALGG
