(data stored in ACNUC7421 zone)

SWISSPROT: AROL_SALTY

ID   AROL_SALTY              Reviewed;         181 AA.
AC   P63603; Q8XEP9;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 90.
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=STM0388;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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}.
DR   EMBL; AE006468; AAL19342.1; -; Genomic_DNA.
DR   RefSeq; NP_459383.1; NC_003197.2.
DR   RefSeq; WP_000983569.1; NC_003197.2.
DR   SMR; P63603; -.
DR   PaxDb; P63603; -.
DR   EnsemblBacteria; AAL19342; AAL19342; STM0388.
DR   GeneID; 1251907; -.
DR   KEGG; stm:STM0388; -.
DR   PATRIC; fig|99287.12.peg.413; -.
DR   eggNOG; ENOG4105KHV; Bacteria.
DR   eggNOG; COG0703; LUCA.
DR   HOGENOM; HOG000032568; -.
DR   KO; K00891; -.
DR   OMA; DTDIFMQ; -.
DR   PhylomeDB; P63603; -.
DR   BioCyc; SENT99287:STM0388-MONOMER; -.
DR   UniPathway; UPA00053; UER00088.
DR   Proteomes; UP000001014; 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; IBA:GO_Central.
DR   GO; GO:0004765; F:shikimate kinase activity; IBA:GO_Central.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019632; P:shikimate metabolic process; IBA:GO_Central.
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; P63603.
DR   SWISS-2DPAGE; P63603.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; ATP-binding;
KW   Cytoplasm; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..181
FT                   /note="Shikimate kinase 2"
FT                   /id="PRO_0000192407"
FT   NP_BIND         12..17
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01269"
FT   REGION          112..126
FT                   /note="LID domain"
FT   METAL           16
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01269"
FT   METAL           32
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01269"
FT   BINDING         34
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01269"
FT   BINDING         58
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01269"
FT   BINDING         79
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01269"
FT   BINDING         120
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01269"
FT   BINDING         139
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01269"
SQ   SEQUENCE   181 AA;  19804 MW;  F2C4B2C36445C54C CRC64;
     MMQPLYLVGP RGCGKTTIGM ALAQATGFRF ADTDRWLQSH VQMSVADIVE KEGWGGFRAR
     ETAALEAVSA PSTVVATGGG IILTEYNRRY MHRVGVVIYL CAPVSTLVNR LEAEPEADLR
     PTLTGKPLSE EVREVLEQRD ALYRETAHYI IDATKAPAQV VSEIIAALPP STQRLQGDVY
     T
//

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