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Database: UniProt
Entry: E4RYA3_LEAB4
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ID   E4RYA3_LEAB4            Unreviewed;       177 AA.
AC   E4RYA3;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 73.
DE   RecName: Full=Shikimate kinase {ECO:0000256|HAMAP-Rule:MF_00109};
DE            Short=SK {ECO:0000256|HAMAP-Rule:MF_00109};
DE            EC=2.7.1.71 {ECO:0000256|HAMAP-Rule:MF_00109};
GN   Name=aroK {ECO:0000256|HAMAP-Rule:MF_00109};
GN   OrderedLocusNames=Lbys_1606 {ECO:0000313|EMBL:ADQ17314.1};
OS   Leadbetterella byssophila (strain DSM 17132 / JCM 16389 / KACC 11308 / NBRC
OS   106382 / 4M15).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Leadbetterella.
OX   NCBI_TaxID=649349 {ECO:0000313|EMBL:ADQ17314.1, ECO:0000313|Proteomes:UP000007435};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17132;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Teshima H., Brettin T., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA   Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Leadbetterella byssophila DSM 17132.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADQ17314.1, ECO:0000313|Proteomes:UP000007435}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17132 / JCM 16389 / KACC 11308 / NBRC 106382 / 4M15
RC   {ECO:0000313|Proteomes:UP000007435};
RX   PubMed=21475582; DOI=10.4056/sigs.1413518;
RA   Abt B., Teshima H., Lucas S., Lapidus A., Del Rio T.G., Nolan M., Tice H.,
RA   Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K.,
RA   Pati A., Tapia R., Han C., Goodwin L., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M., Tindall B.J.,
RA   Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Leadbetterella byssophila type strain
RT   (4M15).";
RL   Stand. Genomic Sci. 4:2-12(2011).
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|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|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}.
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DR   EMBL; CP002305; ADQ17314.1; -; Genomic_DNA.
DR   RefSeq; WP_013408363.1; NC_014655.1.
DR   AlphaFoldDB; E4RYA3; -.
DR   STRING; 649349.Lbys_1606; -.
DR   KEGG; lby:Lbys_1606; -.
DR   eggNOG; COG0703; Bacteria.
DR   HOGENOM; CLU_057607_4_0_10; -.
DR   OMA; EVRDPLY; -.
DR   OrthoDB; 9800332at2; -.
DR   UniPathway; UPA00053; UER00088.
DR   Proteomes; UP000007435; 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: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   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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00109};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00109};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00109};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00109};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00109, ECO:0000313|EMBL:ADQ17314.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00109};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00109};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00109};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007435};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00109, ECO:0000313|EMBL:ADQ17314.1}.
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         80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT   BINDING         120
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
SQ   SEQUENCE   177 AA;  20304 MW;  D056E7F76F6D75D0 CRC64;
     MTTNIFMIGM PSSGKSTLGR QLAKELNYEF IDLDKKIELA EGRKISEIFN LEGEEYFRKI
     ETEHLKRIEP NSRLVIATGG GTPCNGNNMD FIKENGISVF LDVKPKKLEE RMRNSKKNNR
     PLYNLESELL VDTLTKTYED RIETYKRADI VIEGDTDANT ILWILDAHFS KAVKDVI
//
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