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Database: UniProt/TrEMBL
Entry: E8T9G2_MESCW
LinkDB: E8T9G2_MESCW
Original site: E8T9G2_MESCW 
ID   E8T9G2_MESCW            Unreviewed;       203 AA.
AC   E8T9G2;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   11-JUN-2014, entry version 24.
DE   RecName: Full=Shikimate kinase;
DE            Short=SK;
DE            EC=2.7.1.71;
GN   Name=aroK; OrderedLocusNames=Mesci_1507;
OS   Mesorhizobium ciceri bv. biserrulae (strain HAMBI 2942 / LMG 23838 /
OS   WSM1271).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=765698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAMBI 2942 / LMG 23838 / WSM1271;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Nandasena K., Reeve W.G.,
RA   Howieson J.G., O'Hara G., Tiwari R.P., Woyke T.;
RT   "Complete sequence of chromosome of Mesorhizobium ciceri bv.
RT   biserrulae WSM1271.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl
CC       group of shikimic acid using ATP as a cosubstrate (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 5/7.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the shikimate kinase family.
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DR   EMBL; CP002447; ADV10665.1; -; Genomic_DNA.
DR   RefSeq; YP_004140715.1; NC_014923.1.
DR   EnsemblBacteria; ADV10665; ADV10665; Mesci_1507.
DR   GeneID; 10116958; -.
DR   KEGG; mci:Mesci_1507; -.
DR   PATRIC; 45252920; VBIMesCic160642_1949.
DR   HOGENOM; HOG000032568; -.
DR   KO; K00891; -.
DR   OMA; VWLKAEL; -.
DR   BioCyc; MCIC765698:GHQ5-1519-MONOMER; -.
DR   UniPathway; UPA00053; UER00088.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00109; Shikimate_kinase; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000623; Shikimate_kinase/TSH1.
DR   InterPro; IPR023000; Shikimate_kinase_CS.
DR   Pfam; PF01202; SKI; 1.
DR   PRINTS; PR01100; SHIKIMTKNASE.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS01128; SHIKIMATE_KINASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Transferase.
FT   NP_BIND      32     37       ATP (By similarity){EA10}.
FT   METAL        36     36       Magnesium (By similarity){EA10}.
FT   BINDING      54     54       Substrate (By similarity){EA10}.
FT   BINDING      78     78       Substrate (By similarity){EA10}.
FT   BINDING     100    100       Substrate; via amide nitrogen (By
FT                                similarity){EA10}.
FT   BINDING     138    138       ATP (By similarity){EA10}.
FT   BINDING     157    157       Substrate (By similarity){EA10}.
FT   BINDING     174    174       ATP (By similarity){EA10}.
SQ   SEQUENCE   203 AA;  22184 MW;  B15E60ED5A0EB7D0 CRC64;
     MNALPANPPD ENHAALLGRL GSRSVVFVGL MGAGKTAIGR KVATMLALPF IDSDQEIESV
     SRMTVPELFE RYGETEFRAL EQRVILRVLE NGPQVLSTGG GAFMNAQTRE AIAAHGVSVW
     LKAELDLLMD RVAKKQNRPL LKSADPRAVL ERLMGERYPV YATSDVTVPT RDDRKEVIAT
     EVVDALCRHF GIDQAAATGE VEQ
//
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