AROK_BORBR
ID AROK_BORBR Reviewed; 211 AA.
AC Q7WR85;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=BB0071;
OS Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS (Alcaligenes bronchisepticus).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(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; BX640437; CAE30573.1; -; Genomic_DNA.
DR RefSeq; WP_010925692.1; NC_002927.3.
DR AlphaFoldDB; Q7WR85; -.
DR SMR; Q7WR85; -.
DR STRING; 257310.BB0071; -.
DR EnsemblBacteria; CAE30573; CAE30573; BB0071.
DR KEGG; bbr:BB0071; -.
DR eggNOG; COG0703; Bacteria.
DR HOGENOM; CLU_057607_2_2_4; -.
DR OMA; IGKHLFE; -.
DR OrthoDB; 1392851at2; -.
DR UniPathway; UPA00053; UER00088.
DR Proteomes; UP000001027; 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 Transferase.
FT CHAIN 1..211
FT /note="Shikimate kinase"
FT /id="PRO_0000237850"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT BINDING 54
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT BINDING 118
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"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
SQ SEQUENCE 211 AA; 23083 MW; EB8502512BFBD5EA CRC64;
MNASANLCAA SDNDPQPGDQ EAAHPVACAG DEPAAFLPHD LPIFLVGMMG AGKTTIGRGL
ARALRREFID LDHELEARCG VRVPVIFEIE GEAGFRRREA AALQECTQRR QIILATGGGA
VLAAENRQAL RERGIVIYLR ASVEELFRRT SRDRNRPLLA TADPRATLRE LMVAREPLYN
EVADLVIDTG SMPIATLVKS LLPKLQAYEK K
