AROL_SALTI
ID AROL_SALTI Reviewed; 181 AA.
AC P63604; Q8XEP9;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Shikimate kinase 2 {ECO:0000255|HAMAP-Rule:MF_01269};
DE Short=SK 2 {ECO:0000255|HAMAP-Rule:MF_01269};
DE EC=2.7.1.71 {ECO:0000255|HAMAP-Rule:MF_01269};
GN Name=aroL {ECO:0000255|HAMAP-Rule:MF_01269};
GN OrderedLocusNames=STY0421, t2476;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(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_01269}.
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_01269};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01269};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01269};
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_01269}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01269}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01269}.
CC -!- DOMAIN: The LID domain closes over the active site upon ATP binding.
CC {ECO:0000255|HAMAP-Rule:MF_01269}.
CC -!- SIMILARITY: Belongs to the shikimate kinase family. AroL subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01269}.
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DR EMBL; AL513382; CAD08843.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO70064.1; -; Genomic_DNA.
DR RefSeq; NP_454983.1; NC_003198.1.
DR RefSeq; WP_000983569.1; NZ_WSUR01000017.1.
DR AlphaFoldDB; P63604; -.
DR SMR; P63604; -.
DR STRING; 220341.16501657; -.
DR EnsemblBacteria; AAO70064; AAO70064; t2476.
DR KEGG; stt:t2476; -.
DR KEGG; sty:STY0421; -.
DR PATRIC; fig|220341.7.peg.419; -.
DR eggNOG; COG0703; Bacteria.
DR HOGENOM; CLU_057607_4_3_6; -.
DR OMA; DTDIFMQ; -.
DR UniPathway; UPA00053; UER00088.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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 HAMAP; MF_01269; Shikimate_kinase_2; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR031322; Shikimate/glucono_kinase.
DR InterPro; IPR000623; Shikimate_kinase/TSH1.
DR InterPro; IPR027544; Shikimate_kinase_2.
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..181
FT /note="Shikimate kinase 2"
FT /id="PRO_0000192405"
FT REGION 112..126
FT /note="LID domain"
FT BINDING 12..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01269"
FT BINDING 16
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01269"
FT BINDING 32
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01269"
FT BINDING 34
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01269"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01269"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01269"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01269"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01269"
SQ SEQUENCE 181 AA; 19804 MW; F2C4B2C36445C54C CRC64;
MMQPLYLVGP RGCGKTTIGM ALAQATGFRF ADTDRWLQSH VQMSVADIVE KEGWGGFRAR
ETAALEAVSA PSTVVATGGG IILTEYNRRY MHRVGVVIYL CAPVSTLVNR LEAEPEADLR
PTLTGKPLSE EVREVLEQRD ALYRETAHYI IDATKAPAQV VSEIIAALPP STQRLQGDVY
T
