AROK_ECOLI
ID AROK_ECOLI Reviewed; 173 AA.
AC P0A6D7; P24167; P78113; Q2M755; Q8X4S0;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Shikimate kinase 1;
DE Short=SK 1;
DE EC=2.7.1.71;
DE AltName: Full=Shikimate kinase I;
DE Short=SKI;
GN Name=aroK; OrderedLocusNames=b3390, JW5947;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K12;
RX PubMed=1309529; DOI=10.1128/jb.174.2.525-529.1992;
RA Lobner-Olesen A., Boye E., Marinus M.G.;
RT "Identification of the gene (aroK) encoding shikimic acid kinase I of
RT Escherichia coli.";
RL J. Bacteriol. 174:525-529(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1630320; DOI=10.1111/j.1365-2958.1992.tb01356.x;
RA Lobner-Olesen A., Boye E., Marinus M.G.;
RT "Expression of the Escherichia coli dam gene.";
RL Mol. Microbiol. 6:1841-1851(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=7612934; DOI=10.3109/10425179509029363;
RA Griffin H.G., Gasson M.J.;
RT "The gene (aroK) encoding shikimate kinase I from Escherichia coli.";
RL DNA Seq. 5:195-197(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=7883721; DOI=10.1128/jb.177.6.1627-1629.1995;
RA Whipp M.J., Pittard A.J.;
RT "A reassessment of the relationship between aroK- and aroL-encoded
RT shikimate kinase enzymes of Escherichia coli.";
RL J. Bacteriol. 177:1627-1629(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7603433; DOI=10.1007/bf00290345;
RA Lyngstadaas A., Lobner-Olesen A., Boye E.;
RT "Characterization of three genes in the dam-containing operon of
RT Escherichia coli.";
RL Mol. Gen. Genet. 247:546-554(1995).
RN [6]
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 [7]
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 [8]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [9]
RP PROTEIN SEQUENCE OF 2-5.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [10]
RP KINETIC PARAMETERS.
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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS), AND SUBUNIT.
RX PubMed=12001235; DOI=10.1002/prot.10099.abs;
RA Romanowski M.J., Burley S.K.;
RT "Crystal structure of the Escherichia coli shikimate kinase I (AroK) that
RT confers sensitivity to mecillinam.";
RL Proteins 47:558-562(2002).
CC -!- FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl
CC group of shikimic acid using ATP as a cosubstrate.
CC {ECO:0000269|PubMed:1309529}.
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000305};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20 mM for shikimate {ECO:0000269|PubMed:3001029};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 5/7.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12001235}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Constitutively expressed.
CC -!- DOMAIN: The LID domain closes over the active site upon ATP binding.
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. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58187.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC36834.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA79665.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M76389; AAC36834.1; ALT_FRAME; Unassigned_DNA.
DR EMBL; X80167; CAA56448.1; -; Genomic_DNA.
DR EMBL; L39822; AAB59099.1; -; Genomic_DNA.
DR EMBL; Z19601; CAA79665.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U18997; AAA58187.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76415.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77901.1; -; Genomic_DNA.
DR PIR; A65134; A65134.
DR RefSeq; WP_000818618.1; NZ_STEB01000004.1.
DR RefSeq; YP_026215.2; NC_000913.3.
DR PDB; 1KAG; X-ray; 2.05 A; A/B=1-173.
DR PDBsum; 1KAG; -.
DR AlphaFoldDB; P0A6D7; -.
DR SMR; P0A6D7; -.
DR BioGRID; 4259297; 212.
DR DIP; DIP-48271N; -.
DR IntAct; P0A6D7; 1.
DR STRING; 511145.b3390; -.
DR SWISS-2DPAGE; P0A6D7; -.
DR jPOST; P0A6D7; -.
DR PaxDb; P0A6D7; -.
DR PRIDE; P0A6D7; -.
DR EnsemblBacteria; AAC76415; AAC76415; b3390.
DR EnsemblBacteria; BAE77901; BAE77901; BAE77901.
DR GeneID; 2847759; -.
DR GeneID; 67417016; -.
DR KEGG; ecj:JW5947; -.
DR KEGG; eco:b3390; -.
DR PATRIC; fig|1411691.4.peg.3340; -.
DR EchoBASE; EB0079; -.
DR eggNOG; COG0703; Bacteria.
DR HOGENOM; CLU_057607_2_2_6; -.
DR InParanoid; P0A6D7; -.
DR OMA; IGKHLFE; -.
DR PhylomeDB; P0A6D7; -.
DR BioCyc; EcoCyc:AROK-MON; -.
DR BioCyc; MetaCyc:AROK-MON; -.
DR BRENDA; 2.7.1.71; 2026.
DR UniPathway; UPA00053; UER00088.
DR EvolutionaryTrace; P0A6D7; -.
DR PRO; PR:P0A6D7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
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; IDA:EcoCyc.
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; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
DR CDD; cd00464; SK; 1.
DR Gene3D; 3.40.50.300; -; 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 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 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646,
FT ECO:0000269|PubMed:9600841"
FT CHAIN 2..173
FT /note="Shikimate kinase 1"
FT /id="PRO_0000192377"
FT REGION 116..127
FT /note="Lid domain"
FT BINDING 14..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 18
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 82
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 140
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:1KAG"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:1KAG"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:1KAG"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:1KAG"
FT HELIX 47..71
FT /evidence="ECO:0007829|PDB:1KAG"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:1KAG"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:1KAG"
FT HELIX 88..97
FT /evidence="ECO:0007829|PDB:1KAG"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:1KAG"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:1KAG"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:1KAG"
FT HELIX 130..147
FT /evidence="ECO:0007829|PDB:1KAG"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:1KAG"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:1KAG"
SQ SEQUENCE 173 AA; 19538 MW; 5681B562B5CD4674 CRC64;
MAEKRNIFLV GPMGAGKSTI GRQLAQQLNM EFYDSDQEIE KRTGADVGWV FDLEGEEGFR
DREEKVINEL TEKQGIVLAT GGGSVKSRET RNRLSARGVV VYLETTIEKQ LARTQRDKKR
PLLHVETPPR EVLEALANER NPLYEEIADV TIRTDDQSAK VVANQIIHML ESN
