(data stored in ACNUC7421 zone)

SWISSPROT: AROL_ECODH

ID   AROL_ECODH              Reviewed;         174 AA.
AC   B1XEX7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 54.
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=ECDH10B_0345;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
CC   -!- FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl
CC       group of shikimic acid using ATP as a cosubstrate.
CC       {ECO:0000255|HAMAP-Rule:MF_01269}.
CC   -!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate.
CC       {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-
CC       Rule:MF_01269};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 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
CC       binding. {ECO:0000255|HAMAP-Rule:MF_01269}.
CC   -!- SIMILARITY: Belongs to the shikimate kinase family. AroL
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01269}.
DR   EMBL; CP000948; ACB01517.1; -; Genomic_DNA.
DR   RefSeq; WP_000193393.1; NC_010473.1.
DR   ProteinModelPortal; B1XEX7; -.
DR   SMR; B1XEX7; -.
DR   EnsemblBacteria; ACB01517; ACB01517; ECDH10B_0345.
DR   KEGG; ecd:ECDH10B_0345; -.
DR   eggNOG; ENOG4105KHV; Bacteria.
DR   eggNOG; COG0703; LUCA.
DR   HOGENOM; HOG000032568; -.
DR   KO; K00891; -.
DR   OMA; KHLFERS; -.
DR   UniPathway; UPA00053; UER00088.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00464; SK; 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;
DR   PRODOM; B1XEX7.
DR   SWISS-2DPAGE; B1XEX7.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Transferase.
FT   CHAIN         1    174       Shikimate kinase 2.
FT                                /FTId=PRO_1000140131.
FT   NP_BIND      12     17       ATP. {ECO:0000255|HAMAP-Rule:MF_01269}.
FT   REGION      112    126       LID domain.
FT   METAL        16     16       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01269}.
FT   METAL        32     32       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01269}.
FT   BINDING      34     34       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01269}.
FT   BINDING      58     58       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01269}.
FT   BINDING      79     79       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01269}.
FT   BINDING     120    120       ATP. {ECO:0000255|HAMAP-Rule:MF_01269}.
FT   BINDING     139    139       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01269}.
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
//

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