(data stored in ACNUC7421 zone)

SWISSPROT: AROK_PSEPF

ID   AROK_PSEPF              Reviewed;         172 AA.
AC   Q3KJA2;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 95.
DE   RecName: Full=Shikimate kinase {ECO:0000255|HAMAP-Rule:MF_00109};
DE            Short=SK {ECO:0000255|HAMAP-Rule:MF_00109};
DE            EC=2.7.1.71 {ECO:0000255|HAMAP-Rule:MF_00109};
GN   Name=aroK {ECO:0000255|HAMAP-Rule:MF_00109};
GN   OrderedLocusNames=Pfl01_0410;
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
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_00109}.
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_00109};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00109};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00109};
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_00109}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00109}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00109}.
CC   -!- SIMILARITY: Belongs to the shikimate kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00109}.
DR   EMBL; CP000094; ABA72154.1; -; Genomic_DNA.
DR   RefSeq; WP_011332081.1; NC_007492.2.
DR   SMR; Q3KJA2; -.
DR   STRING; 205922.Pfl01_0410; -.
DR   PRIDE; Q3KJA2; -.
DR   EnsemblBacteria; ABA72154; ABA72154; Pfl01_0410.
DR   KEGG; pfo:Pfl01_0410; -.
DR   eggNOG; ENOG4105KHV; Bacteria.
DR   eggNOG; COG0703; LUCA.
DR   HOGENOM; HOG000032568; -.
DR   KO; K00891; -.
DR   OMA; VLIGMMG; -.
DR   BioCyc; PFLU205922:G1G4S-414-MONOMER; -.
DR   UniPathway; UPA00053; UER00088.
DR   Proteomes; UP000002704; 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   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   3: Inferred from homology;
DR   PRODOM; Q3KJA2.
DR   SWISS-2DPAGE; Q3KJA2.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Transferase.
FT   CHAIN         1    172       Shikimate kinase.
FT                                /FTId=PRO_0000237913.
FT   NP_BIND      11     16       ATP. {ECO:0000255|HAMAP-Rule:MF_00109}.
FT   METAL        15     15       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00109}.
FT   BINDING      33     33       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00109}.
FT   BINDING      57     57       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00109}.
FT   BINDING      79     79       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00109}.
FT   BINDING     117    117       ATP. {ECO:0000255|HAMAP-Rule:MF_00109}.
FT   BINDING     136    136       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00109}.
FT   BINDING     153    153       ATP. {ECO:0000255|HAMAP-Rule:MF_00109}.
SQ   SEQUENCE   172 AA;  19274 MW;  3F79BBFDC573CB18 CRC64;
     MRNLILVGPM GAGKSTIGRL LAKELRLPFK DSDKEIELRT GANIPWIFDK EGEPGFRDRE
     QAMIAELCAF DGVVLATGGG AVMRDANRKA LHEGGRVVYL HASVEQQVGR TSRDRNRPLL
     RTANPEKTLR DLLAIRDPLY REIADLVVET DERPPRMVVL DILDRLAQLP PR
//

If you have problems or comments...

PBIL Back to PBIL home page