ID E8T9G2_MESCW Unreviewed; 203 AA.
AC E8T9G2;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 01-MAY-2013, entry version 18.
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; ADIPWIF; -.
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:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0004765; F:shikimate kinase activity; IEA:HAMAP.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:HAMAP.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_00109; Shikimate_kinase; 1; -.
DR InterPro; IPR000623; Shikimate_kinase.
DR InterPro; IPR023000; Shikimate_kinase_CS.
DR Pfam; PF01202; SKI; 1.
DR PRINTS; PR01100; SHIKIMTKNASE.
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).
FT METAL 36 36 Magnesium (By similarity).
FT BINDING 54 54 Substrate (By similarity).
FT BINDING 78 78 Substrate (By similarity).
FT BINDING 100 100 Substrate; via amide nitrogen (By
FT similarity).
FT BINDING 138 138 ATP (By similarity).
FT BINDING 157 157 Substrate (By similarity).
FT BINDING 174 174 ATP (By similarity).
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
//
