AROL_ECOLI
ID AROL_ECOLI Reviewed; 174 AA.
AC P0A6E1; P08329; Q2MC37;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Shikimate kinase 2;
DE Short=SK 2;
DE EC=2.7.1.71 {ECO:0000269|PubMed:3001029};
DE AltName: Full=Shikimate kinase II;
DE Short=SKII;
GN Name=aroL; OrderedLocusNames=b0388, JW0379;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-25, FUNCTION, AND
RP SUBUNIT.
RC STRAIN=K12;
RX PubMed=3026317; DOI=10.1042/bj2370427;
RA Millar G., Lewendon A., Hunter M.G., Coggins J.R.;
RT "The cloning and expression of the aroL gene from Escherichia coli K12.
RT Purification and complete amino acid sequence of shikimate kinase II, the
RT aroL-gene product.";
RL Biochem. J. 237:427-437(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3001025; DOI=10.1128/jb.165.1.233-239.1986;
RA Defeyter R.C., Davidson B.E., Pittard J.;
RT "Nucleotide sequence of the transcription unit containing the aroL and aroM
RT genes from Escherichia coli K-12.";
RL J. Bacteriol. 165:233-239(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 2-9, FUNCTION, COFACTOR, KINETIC PARAMETERS, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=K12;
RX PubMed=3001029; DOI=10.1128/jb.165.1.331-333.1986;
RA DeFeyter R.C., Pittard J.;
RT "Purification and properties of shikimate kinase II from Escherichia coli
RT K-12.";
RL J. Bacteriol. 165:331-333(1986).
RN [7]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=3001024; DOI=10.1128/jb.165.1.226-232.1986;
RA DeFeyter R.C., Pittard J.;
RT "Genetic and molecular analysis of aroL, the gene for shikimate kinase II
RT in Escherichia coli K-12.";
RL J. Bacteriol. 165:226-232(1986).
RN [8]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=1530846; DOI=10.1128/jb.174.1.331-335.1992;
RA Heatwole V.M., Somerville R.L.;
RT "Synergism between the Trp repressor and Tyr repressor in repression of the
RT aroL promoter of Escherichia coli K-12.";
RL J. Bacteriol. 174:331-335(1992).
RN [9]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=7961453; DOI=10.1128/jb.176.22.6921-6930.1994;
RA Lawley B., Pittard A.J.;
RT "Regulation of aroL expression by TyrR protein and Trp repressor in
RT Escherichia coli K-12.";
RL J. Bacteriol. 176:6921-6930(1994).
CC -!- FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl
CC group of shikimic acid using ATP as a cosubstrate.
CC {ECO:0000269|PubMed:3001029, ECO:0000269|PubMed:3026317}.
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:0000269|PubMed:3001029};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:3001029};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:3001029};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=200 uM for shikimate {ECO:0000269|PubMed:3001029};
CC KM=160 uM for ATP {ECO:0000269|PubMed:3001029};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 5/7. {ECO:0000305|PubMed:3001029}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:3026317}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Expressed under the control of TyrR and TrpR repressors.
CC {ECO:0000269|PubMed:1530846, ECO:0000269|PubMed:3001024,
CC ECO:0000269|PubMed:7961453}.
CC -!- DOMAIN: The LID domain closes over the active site upon ATP binding.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Two isozymes have been found in E.coli. AroK has 100-
CC fold lower affinity for shikimate than AroL, suggesting that AroL is
CC the dominant enzyme in the biosynthesis of the aromatic amino acids,
CC with AroK playing a secondary role and possibly participating in an as
CC yet unidentified cellular process.
CC -!- SIMILARITY: Belongs to the shikimate kinase family. AroL subfamily.
CC {ECO:0000305}.
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DR EMBL; X04064; CAA27696.1; -; Genomic_DNA.
DR EMBL; M13045; AAA83833.1; -; Genomic_DNA.
DR EMBL; U73857; AAB18112.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73491.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76169.1; -; Genomic_DNA.
DR PIR; A90333; KIECS.
DR RefSeq; NP_414922.1; NC_000913.3.
DR RefSeq; WP_000193393.1; NZ_STEB01000007.1.
DR AlphaFoldDB; P0A6E1; -.
DR SMR; P0A6E1; -.
DR BioGRID; 4259831; 6.
DR IntAct; P0A6E1; 3.
DR STRING; 511145.b0388; -.
DR jPOST; P0A6E1; -.
DR PaxDb; P0A6E1; -.
DR PRIDE; P0A6E1; -.
DR EnsemblBacteria; AAC73491; AAC73491; b0388.
DR EnsemblBacteria; BAE76169; BAE76169; BAE76169.
DR GeneID; 66671313; -.
DR GeneID; 945031; -.
DR KEGG; ecj:JW0379; -.
DR KEGG; eco:b0388; -.
DR PATRIC; fig|1411691.4.peg.1890; -.
DR EchoBASE; EB0080; -.
DR eggNOG; COG0703; Bacteria.
DR HOGENOM; CLU_057607_4_3_6; -.
DR InParanoid; P0A6E1; -.
DR OMA; DTDIFMQ; -.
DR PhylomeDB; P0A6E1; -.
DR BioCyc; EcoCyc:AROL-MON; -.
DR BioCyc; MetaCyc:AROL-MON; -.
DR SABIO-RK; P0A6E1; -.
DR UniPathway; UPA00053; UER00088.
DR PRO; PR:P0A6E1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IDA:EcoCyc.
DR GO; GO:0004765; F:shikimate kinase activity; IDA:EcoCyc.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IMP:EcoliWiki.
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 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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; ATP-binding;
KW Cytoplasm; Direct protein sequencing; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3001029,
FT ECO:0000269|PubMed:3026317"
FT CHAIN 2..174
FT /note="Shikimate kinase 2"
FT /id="PRO_0000192378"
FT REGION 112..126
FT /note="LID domain"
FT BINDING 12..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 16
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 32
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 174 AA; 19151 MW; FCB8D86F6DD55347 CRC64;
MTQPLFLIGP RGCGKTTVGM ALADSLNRRF VDTDQWLQSQ LNMTVAEIVE REEWAGFRAR
ETAALEAVTA PSTVIATGGG IILTEFNRHF MQNNGIVVYL CAPVSVLVNR LQAAPEEDLR
PTLTGKPLSE EVQEVLEERD ALYREVAHII IDATNEPSQV ISEIRSALAQ TINC
