AROL_ECOUT
ID AROL_ECOUT Reviewed; 174 AA.
AC Q1RFF6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
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}; OrderedLocusNames=UTI89_C0407;
OS Escherichia coli (strain UTI89 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=364106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTI89 / UPEC;
RX PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA Gordon J.I.;
RT "Identification of genes subject to positive selection in uropathogenic
RT strains of Escherichia coli: a comparative genomics approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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; CP000243; ABE05908.1; -; Genomic_DNA.
DR RefSeq; WP_000193383.1; NC_007946.1.
DR AlphaFoldDB; Q1RFF6; -.
DR SMR; Q1RFF6; -.
DR EnsemblBacteria; ABE05908; ABE05908; UTI89_C0407.
DR KEGG; eci:UTI89_C0407; -.
DR HOGENOM; CLU_057607_4_3_6; -.
DR OMA; DTDIFMQ; -.
DR UniPathway; UPA00053; UER00088.
DR Proteomes; UP000001952; 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..174
FT /note="Shikimate kinase 2"
FT /id="PRO_1000067331"
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 174 AA; 19136 MW; FCAD02509EFF7A47 CRC64;
MTQPLFLIGP RGCGKTTVGM ALADSLNRRF VDTDLWLQSQ LNMTVAEIVE REEWAGFRAR
ETAALEAVTA PSTVIATGGG IILTEFNRHF MQNNGIVVYL CAPVSVLVNR LQAAPEEDLR
PTLTGKPLSE EVQEVLEERD ALYREVAHII IDATNEPSQV ISEIRSALAQ TINC
