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Entry: A0A1M5CU05_9BACT
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ID   A0A1M5CU05_9BACT        Unreviewed;       187 AA.
AC   A0A1M5CU05;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Shikimate kinase {ECO:0000256|ARBA:ARBA00012154, ECO:0000256|HAMAP-Rule:MF_00109};
DE            Short=SK {ECO:0000256|HAMAP-Rule:MF_00109};
DE            EC=2.7.1.71 {ECO:0000256|ARBA:ARBA00012154, ECO:0000256|HAMAP-Rule:MF_00109};
GN   Name=aroK {ECO:0000256|HAMAP-Rule:MF_00109};
GN   ORFNames=SAMN05443144_11089 {ECO:0000313|EMBL:SHF58204.1};
OS   Fodinibius roseus.
OC   Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Fodinibius.
OX   NCBI_TaxID=1194090 {ECO:0000313|EMBL:SHF58204.1, ECO:0000313|Proteomes:UP000184041};
RN   [1] {ECO:0000313|EMBL:SHF58204.1, ECO:0000313|Proteomes:UP000184041}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21986 {ECO:0000313|EMBL:SHF58204.1,
RC   ECO:0000313|Proteomes:UP000184041};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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:0000256|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:0000256|ARBA:ARBA00000172,
CC         ECO:0000256|HAMAP-Rule:MF_00109};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00109};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|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:0000256|ARBA:ARBA00004842, ECO:0000256|HAMAP-Rule:MF_00109}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00109}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00109}.
CC   -!- SIMILARITY: Belongs to the shikimate kinase family.
CC       {ECO:0000256|ARBA:ARBA00006997, ECO:0000256|HAMAP-Rule:MF_00109}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00109}.
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DR   EMBL; FQUS01000010; SHF58204.1; -; Genomic_DNA.
DR   RefSeq; WP_073063728.1; NZ_FQUS01000010.1.
DR   AlphaFoldDB; A0A1M5CU05; -.
DR   STRING; 1194090.SAMN05443144_11089; -.
DR   OrthoDB; 9800332at2; -.
DR   UniPathway; UPA00053; UER00088.
DR   Proteomes; UP000184041; Unassembled WGS sequence.
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:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
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; P-loop containing nucleotide triphosphate hydrolases; 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   PANTHER; PTHR21087; SHIKIMATE KINASE; 1.
DR   PANTHER; PTHR21087:SF16; SHIKIMATE KINASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF01202; SKI; 1.
DR   PRINTS; PR01100; SHIKIMTKNASE.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS01128; SHIKIMATE_KINASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00109};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|HAMAP-Rule:MF_00109};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00109}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00109};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00109};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00109};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00109};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00109}; Reference proteome {ECO:0000313|Proteomes:UP000184041};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00109}.
FT   BINDING         18..23
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT   BINDING         22
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT   BINDING         40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT   BINDING         124
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
SQ   SEQUENCE   187 AA;  20730 MW;  A3E293EB9666B8FF CRC64;
     MDIDGEISEV IFLCGFMGAG KTTIGQKLAA ELGRPFLDLD DRIVEKAGKP IPEIFEASGE
     GRFRAIERSA LLEVARQFNG VVALGGGSLQ NQHLLDHLKC NGLLIFIEAP IPVIIDRISQ
     DANRPLLLDE QGEPKDRDTL KKELKMLYED RLPLYEQAMI TLNIKAGESA DQQVKTLINK
     IRNYVAS
//
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