AROK_BACTN
ID AROK_BACTN Reviewed; 175 AA.
AC Q8A2B2;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=BT_3393;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(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}.
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; AE015928; AAO78499.1; -; Genomic_DNA.
DR RefSeq; NP_812305.1; NC_004663.1.
DR RefSeq; WP_008767597.1; NC_004663.1.
DR PDB; 3VAA; X-ray; 1.70 A; A/B/C=1-175.
DR PDBsum; 3VAA; -.
DR AlphaFoldDB; Q8A2B2; -.
DR SMR; Q8A2B2; -.
DR STRING; 226186.BT_3393; -.
DR PaxDb; Q8A2B2; -.
DR PRIDE; Q8A2B2; -.
DR EnsemblBacteria; AAO78499; AAO78499; BT_3393.
DR GeneID; 60924572; -.
DR KEGG; bth:BT_3393; -.
DR PATRIC; fig|226186.12.peg.3461; -.
DR eggNOG; COG0703; Bacteria.
DR HOGENOM; CLU_057607_4_0_10; -.
DR InParanoid; Q8A2B2; -.
DR OMA; IGKHLFE; -.
DR UniPathway; UPA00053; UER00088.
DR Proteomes; UP000001414; 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 Pfam; PF01202; SKI; 1.
DR SUPFAM; SSF52540; SSF52540; 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..175
FT /note="Shikimate kinase"
FT /id="PRO_0000237844"
FT BINDING 11..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT BINDING 15
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT BINDING 33
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT BINDING 118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:3VAA"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:3VAA"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:3VAA"
FT HELIX 32..40
FT /evidence="ECO:0007829|PDB:3VAA"
FT HELIX 44..67
FT /evidence="ECO:0007829|PDB:3VAA"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:3VAA"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3VAA"
FT HELIX 87..94
FT /evidence="ECO:0007829|PDB:3VAA"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:3VAA"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:3VAA"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:3VAA"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:3VAA"
FT HELIX 126..144
FT /evidence="ECO:0007829|PDB:3VAA"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:3VAA"
FT HELIX 159..172
FT /evidence="ECO:0007829|PDB:3VAA"
SQ SEQUENCE 175 AA; 20504 MW; 8309087AFDDBE6B9 CRC64;
MVRIFLTGYM GAGKTTLGKA FARKLNVPFI DLDWYIEERF HKTVGELFTE RGEAGFRELE
RNMLHEVAEF ENVVISTGGG APCFYDNMEF MNRTGKTVFL NVHPDVLFRR LRIAKQQRPI
LQGKEDDELM DFIIQALEKR APFYTQAQYI FNADELEDRW QIESSVQRLQ ELLEL
