(data stored in ACNUC10821 zone)

SWISSPROT: C8U274_ECO10

ID   C8U274_ECO10            Unreviewed;       174 AA.
AC   C8U274;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 70.
DE   RecName: Full=Shikimate kinase 2 {ECO:0000256|HAMAP-Rule:MF_01269, ECO:0000256|SAAS:SAAS01080199};
DE            Short=SK 2 {ECO:0000256|HAMAP-Rule:MF_01269};
DE            EC=2.7.1.71 {ECO:0000256|HAMAP-Rule:MF_01269, ECO:0000256|SAAS:SAAS01157069};
GN   Name=aroL {ECO:0000256|HAMAP-Rule:MF_01269,
GN   ECO:0000313|EMBL:BAI29232.1};
GN   OrderedLocusNames=ECO103_0363 {ECO:0000313|EMBL:BAI29232.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29232.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29232.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl
CC       group of shikimic acid using ATP as a cosubstrate.
CC       {ECO:0000256|HAMAP-Rule:MF_01269, ECO:0000256|SAAS:SAAS01080160}.
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:0000256|HAMAP-Rule:MF_01269,
CC         ECO:0000256|SAAS:SAAS01117062};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01269};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01269,
CC       ECO:0000256|SAAS:SAAS01080056}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01269,
CC       ECO:0000256|SAAS:SAAS01080111}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01269,
CC       ECO:0000256|SAAS:SAAS01080591}.
CC   -!- DOMAIN: The LID domain closes over the active site upon ATP
CC       binding. {ECO:0000256|HAMAP-Rule:MF_01269}.
CC   -!- SIMILARITY: Belongs to the shikimate kinase family. AroL
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01269,
CC       ECO:0000256|SAAS:SAAS01080094}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01269}.
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DR   EMBL; AP010958; BAI29232.1; -; Genomic_DNA.
DR   RefSeq; WP_000193393.1; NC_013353.1.
DR   SMR; C8U274; -.
DR   EnsemblBacteria; BAI29232; BAI29232; ECO103_0363.
DR   KEGG; eoh:ECO103_0363; -.
DR   HOGENOM; HOG000032568; -.
DR   KO; K00891; -.
DR   OMA; DTDIFMQ; -.
DR   BioCyc; ECOL585395:ECO103_RS01900-MONOMER; -.
DR   UniPathway; UPA00053; UER00088.
DR   Proteomes; UP000000959; 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: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; C8U274.
DR   SWISS-2DPAGE; C8U274.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01269,
KW   ECO:0000256|SAAS:SAAS01080173};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01269,
KW   ECO:0000256|SAAS:SAAS01080146};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01269,
KW   ECO:0000256|SAAS:SAAS00728164};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01269,
KW   ECO:0000256|SAAS:SAAS01080576};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01269,
KW   ECO:0000256|SAAS:SAAS00728137, ECO:0000313|EMBL:BAI29232.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01269,
KW   ECO:0000256|SAAS:SAAS01080163};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01269,
KW   ECO:0000256|SAAS:SAAS01080042};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01269,
KW   ECO:0000256|SAAS:SAAS00728079};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01269,
KW   ECO:0000256|SAAS:SAAS00728085}.
FT   NP_BIND      12     17       ATP. {ECO:0000256|HAMAP-Rule:MF_01269}.
FT   REGION      112    126       LID domain. {ECO:0000256|HAMAP-Rule:
FT                                MF_01269}.
FT   METAL        16     16       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01269}.
FT   METAL        32     32       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01269}.
FT   BINDING      34     34       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01269}.
FT   BINDING      58     58       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01269}.
FT   BINDING      79     79       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01269}.
FT   BINDING     120    120       ATP. {ECO:0000256|HAMAP-Rule:MF_01269}.
FT   BINDING     139    139       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                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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