AROK_METS3
ID AROK_METS3 Reviewed; 289 AA.
AC A5ULG2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Shikimate kinase {ECO:0000255|HAMAP-Rule:MF_00370};
DE Short=SK {ECO:0000255|HAMAP-Rule:MF_00370};
DE EC=2.7.1.71 {ECO:0000255|HAMAP-Rule:MF_00370};
GN Name=aroK {ECO:0000255|HAMAP-Rule:MF_00370}; OrderedLocusNames=Msm_0835;
OS Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=420247;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT human gut.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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_00370};
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_00370}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00370}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Archaeal shikimate
CC kinase subfamily. {ECO:0000255|HAMAP-Rule:MF_00370}.
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DR EMBL; CP000678; ABQ87040.1; -; Genomic_DNA.
DR RefSeq; WP_004033093.1; NC_009515.1.
DR AlphaFoldDB; A5ULG2; -.
DR SMR; A5ULG2; -.
DR STRING; 420247.Msm_0835; -.
DR EnsemblBacteria; ABQ87040; ABQ87040; Msm_0835.
DR GeneID; 5217264; -.
DR KEGG; msi:Msm_0835; -.
DR PATRIC; fig|420247.28.peg.832; -.
DR eggNOG; arCOG01025; Archaea.
DR HOGENOM; CLU_073768_0_0_2; -.
DR OMA; WDVLVWT; -.
DR UniPathway; UPA00053; UER00088.
DR Proteomes; UP000001992; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP 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:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.230.10; -; 1.
DR HAMAP; MF_00370; Shik_kinase_arch; 1.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR006203; GHMP_knse_ATP-bd_CS.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR010189; SK_arc.
DR PANTHER; PTHR20861:SF3; PTHR20861:SF3; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF005758; Shikimt_kin_arch; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
DR TIGRFAMs; TIGR01920; Shik_kin_archae; 1.
DR PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; ATP-binding;
KW Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..289
FT /note="Shikimate kinase"
FT /id="PRO_1000059937"
FT BINDING 84..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00370"
SQ SEQUENCE 289 AA; 30581 MW; 443DC4741EC45687 CRC64;
MKKSVRSPGS ATVINAIATG FGAAFGIGLD IKCCANTQNS SITCSNDVGA PTTLMEICAK
KTFEKYGISS DDFGMNFKTE SELPMASGLS SSSALSNAVV SISSKIIAEE FNLMPLDDLE
IINLAIDASL EAKVTITGSF DDATASYFGG VVVTDNKNRK FIIKEKMEEY PVLVYMPNFG
SKSGSSDVGR MKVLSPLVET AFGLARSGDY FKALNLNGLI YANTLGFDSN IAIDALEVGA
IASGLSGTGS SFVAICEDEA IDDIKETWSK YEGRVIETKV DNIGCQFIG