ID B6JAB7_OLICO Unreviewed; 213 AA.
AC B6JAB7;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 01-MAY-2013, entry version 28.
DE RecName: Full=Shikimate kinase;
DE Short=SK;
DE EC=2.7.1.71;
GN Name=aroK; OrderedLocusNames=OCA5_c04330, OCAR_4076;
OS Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Bradyrhizobiaceae; Oligotropha.
OX NCBI_TaxID=504832;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49405 / DSM 1227 / OM5 [Mississippi], and OM5;
RX PubMed=18539730; DOI=10.1128/JB.00614-08;
RA Paul D., Bridges S., Burgess S.C., Dandass Y., Lawrence M.L.;
RT "Genome sequence of the chemolithoautotrophic bacterium Oligotropha
RT carboxidovorans OM5T.";
RL J. Bacteriol. 190:5531-5532(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49405 / DSM 1227 / OM5, and OM5;
RX PubMed=21742883; DOI=10.1128/JB.05619-11;
RA Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G.,
RA Meyer O.;
RT "Complete Genome Sequences of the Chemolithoautotrophic Oligotropha
RT carboxidovorans Strains OM4 and OM5.";
RL J. Bacteriol. 193:5043-5043(2011).
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; CP001196; ACI91227.1; -; Genomic_DNA.
DR EMBL; CP002826; AEI05158.1; -; Genomic_DNA.
DR RefSeq; YP_002287092.1; NC_011386.1.
DR RefSeq; YP_004631399.1; NC_015684.1.
DR STRING; 504832.OCAR_4076; -.
DR EnsemblBacteria; ACI91227; ACI91227; OCAR_4076.
DR EnsemblBacteria; AEI05158; AEI05158; OCA5_c04330.
DR GeneID; 10845565; -.
DR GeneID; 6991539; -.
DR KEGG; oca:OCAR_4076; -.
DR KEGG; ocg:OCA5_c04330; -.
DR PATRIC; 22802161; VBIOliCar134280_0073.
DR eggNOG; COG0703; -.
DR HOGENOM; HOG000032568; -.
DR KO; K00891; -.
DR OMA; ADIPWIF; -.
DR BioCyc; OCAR504832:GJPZ-433-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 42 47 ATP (By similarity).
FT METAL 46 46 Magnesium (By similarity).
FT BINDING 64 64 Substrate (By similarity).
FT BINDING 89 89 Substrate (By similarity).
FT BINDING 111 111 Substrate; via amide nitrogen (By
FT similarity).
FT BINDING 149 149 ATP (By similarity).
FT BINDING 168 168 Substrate (By similarity).
SQ SEQUENCE 213 AA; 23116 MW; 4B4F827226CB1953 CRC64;
MSPDEPAEMP ENLARQGVIQ NQTADILAAL GTRAIVLVGM MGSGKSTVGR RLAARLRLPF
VDADQEIETR HGGMTITEIF ATHGEPYFRE GEAKVISALL DGGAQVLATG GGAFVRDDTR
ERIRSKAVSI WLKADGATVL RRVKRRSDRP LLQTEDPAAT IERLIAAREP FYSLADLTIV
SRDVPHERIV DECIEALHGF LCAAAPVAFA NKT
//
