(data stored in SCRATCH zone)

SWISSPROT: AROK_BACSU

ID   AROK_BACSU              Reviewed;         186 AA.
AC   P37944;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   11-DEC-2019, entry version 127.
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}; Synonyms=aroI;
GN   OrderedLocusNames=BSU03150;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Nakane A., Ogawa K., Nakamura K., Yamane K.;
RT   "Nucleotide sequence of the shikimate kinase gene (aroI) of Bacillus
RT   subtilis.";
RL   J. Ferment. Bioeng. 77:312-314(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Bolotin A.P., Khazak V.E., Gusarov I.I., Stoinova N., Yomantas Y.I.,
RA   Kozlov Y.I.;
RT   "Cloning and nucleotide structure of aroI gene of Bacillus subtilis 168.";
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA   Yamane K., Kumano M., Kurita K.;
RT   "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT   determination of the sequence of a 146 kb segment and identification of 113
RT   genes.";
RL   Microbiology 142:3047-3056(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [5]
RP   SEQUENCE REVISION TO 66.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
CC   -!- FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl
CC       group of shikimic acid using ATP as a cosubstrate. {ECO:0000255|HAMAP-
CC       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-Rule:MF_00109};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       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. {ECO:0000255|HAMAP-
CC       Rule:MF_00109}.
DR   EMBL; D63474; BAA09761.1; -; Genomic_DNA.
DR   EMBL; D50453; BAA08949.1; -; Genomic_DNA.
DR   EMBL; X81355; CAA57123.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12109.2; -; Genomic_DNA.
DR   PIR; I39782; I39782.
DR   RefSeq; NP_388197.2; NC_000964.3.
DR   RefSeq; WP_003246473.1; NZ_JNCM01000030.1.
DR   SMR; P37944; -.
DR   STRING; 224308.BSU03150; -.
DR   PaxDb; P37944; -.
DR   PRIDE; P37944; -.
DR   EnsemblBacteria; CAB12109; CAB12109; BSU03150.
DR   GeneID; 938343; -.
DR   KEGG; bsu:BSU03150; -.
DR   PATRIC; fig|224308.179.peg.329; -.
DR   eggNOG; ENOG4107Z3Y; Bacteria.
DR   eggNOG; COG0703; LUCA.
DR   HOGENOM; HOG000032569; -.
DR   InParanoid; P37944; -.
DR   KO; K00891; -.
DR   OMA; EVRDPLY; -.
DR   PhylomeDB; P37944; -.
DR   BioCyc; BSUB:BSU03150-MONOMER; -.
DR   UniPathway; UPA00053; UER00088.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR   GO; GO:0004765; F:shikimate kinase activity; IBA:GO_Central.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019632; P:shikimate metabolic process; IBA:GO_Central.
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; P37944.
DR   SWISS-2DPAGE; P37944.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; ATP-binding;
KW   Cytoplasm; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..186
FT                   /note="Shikimate kinase"
FT                   /id="PRO_0000192368"
FT   NP_BIND         21..26
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT   METAL           25
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT   BINDING         43
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT   BINDING         67
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT   BINDING         90
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT   BINDING         129
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT   BINDING         147
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00109"
FT   CONFLICT        66
FT                   /note="F -> S (in Ref. 1; BAA09761 and 3; BAA08949)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   186 AA;  21923 MW;  BD4438B5B3AEC3AE CRC64;
     MNAKRAIPVR ERNIVLIGFM GVGKTTIGQL VAKKLYRDFI DIDQQIEKDF NMSIPEIFEK
     KGEDFFRKTE KEYILDICHH KRFKIVSLGG GSFKQEEIRN CCLENCLVLH LDLSWENWKQ
     RADLLIESRP VLHNRSMDEM EQLFNERKVI YDKHNSKVAT DNLSPEEVAD YIVETLKIGW
     DLYQPM
//

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