(data stored in ACNUC7421 zone)

SWISSPROT: AROK_PSEU2

ID   AROK_PSEU2              Reviewed;         172 AA.
AC   Q4ZZE4;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 84.
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=Psyr_0408;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY35478.1; -; Genomic_DNA.
DR   RefSeq; WP_011266378.1; NC_007005.1.
DR   RefSeq; YP_233516.1; NC_007005.1.
DR   SMR; Q4ZZE4; -.
DR   STRING; 205918.Psyr_0408; -.
DR   PRIDE; Q4ZZE4; -.
DR   EnsemblBacteria; AAY35478; AAY35478; Psyr_0408.
DR   GeneID; 3365884; -.
DR   KEGG; psb:Psyr_0408; -.
DR   PATRIC; fig|205918.7.peg.423; -.
DR   eggNOG; ENOG4105KHV; Bacteria.
DR   eggNOG; COG0703; LUCA.
DR   HOGENOM; HOG000032568; -.
DR   KO; K00891; -.
DR   OMA; VLIGMMG; -.
DR   BioCyc; PSYR205918:G1G4J-409-MONOMER; -.
DR   UniPathway; UPA00053; UER00088.
DR   Proteomes; UP000000426; 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; Q4ZZE4.
DR   SWISS-2DPAGE; Q4ZZE4.
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_0000237915.
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;  19129 MW;  F95B31F5F001EA06 CRC64;
     MRNLILVGPM GAGKSTIGRL LAKELRLPFK DSDKEIELRT GANIPWIFDK EGEPGFRDRE
     QAMIAELCAA DGVVLATGGG AVMRSENRHA LRAGGRVVYL HASIEQQVGR TARDRNRPLL
     RTADPARVLS ELLAIRDPFY REIADIVIET DERPPRMVVL EILARLAELP PR
//

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