ID A0A0R1K6T8_9LACO Unreviewed; 262 AA.
AC A0A0R1K6T8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=FD03_GL001691 {ECO:0000313|EMBL:KRK79325.1};
OS Companilactobacillus nodensis DSM 19682 = JCM 14932 = NBRC 107160.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Companilactobacillus.
OX NCBI_TaxID=1423775 {ECO:0000313|EMBL:KRK79325.1, ECO:0000313|Proteomes:UP000051248};
RN [1] {ECO:0000313|EMBL:KRK79325.1, ECO:0000313|Proteomes:UP000051248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19682 {ECO:0000313|EMBL:KRK79325.1,
RC ECO:0000313|Proteomes:UP000051248};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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. {ECO:0000256|HAMAP-
CC Rule:MF_00109}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00109}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRK79325.1}.
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DR EMBL; AZDZ01000019; KRK79325.1; -; Genomic_DNA.
DR RefSeq; WP_025023220.1; NZ_BCWC01000001.1.
DR AlphaFoldDB; A0A0R1K6T8; -.
DR STRING; 1423775.FD03_GL001691; -.
DR PATRIC; fig|1423775.4.peg.1724; -.
DR eggNOG; COG0703; Bacteria.
DR eggNOG; COG1605; Bacteria.
DR OrthoDB; 9800332at2; -.
DR UniPathway; UPA00053; UER00088.
DR Proteomes; UP000051248; 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:0004106; F:chorismate mutase activity; IEA:UniProt.
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; 1.20.59.10; Chorismate mutase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00109; Shikimate_kinase; 1.
DR InterPro; IPR036263; Chorismate_II_sf.
DR InterPro; IPR036979; CM_dom_sf.
DR InterPro; IPR002701; CM_II_prokaryot.
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-RELATED; 1.
DR Pfam; PF01817; CM_2; 1.
DR Pfam; PF01202; SKI; 1.
DR PRINTS; PR01100; SHIKIMTKNASE.
DR SMART; SM00830; CM_2; 1.
DR SUPFAM; SSF48600; Chorismate mutase II; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51168; CHORISMATE_MUT_2; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00109}.
FT DOMAIN 166..258
FT /note="Chorismate mutase"
FT /evidence="ECO:0000259|PROSITE:PS51168"
FT BINDING 12..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 16
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 34
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
SQ SEQUENCE 262 AA; 30024 MW; 7FF265A536ADAD5F CRC64;
MSKTTILIGF MGAGKTTVGK VLANITNQPL LDLDDEFTRG TKLSPKEFME QLGEEEFRTT
ETRILKSQLD FDGIISTGGG VVESELNRQL IRDSSAQVIY LKTSLANVLE RLSHDNVRPM
LRKMSVIDLQ NCWNRRGIFY QLLSNVTIET TNKNPTKIAR EIIDFEQQHD ELLPLRSQID
SLDRQIFNLV SQRFDVVREV ASVKEQLHAS VVQTERMDEV RAELKNDFSD NSNISEQLIE
EMMNILFSSS IQRENEQIKK VD
//
