AROK_METM7
ID AROK_METM7 Reviewed; 283 AA.
AC A6VIV9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=MmarC7_1322;
OS Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=426368;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7 / ATCC BAA-1331;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus maripaludis C7.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000745; ABR66385.1; -; Genomic_DNA.
DR RefSeq; WP_012067852.1; NC_009637.1.
DR AlphaFoldDB; A6VIV9; -.
DR SMR; A6VIV9; -.
DR STRING; 426368.MmarC7_1322; -.
DR EnsemblBacteria; ABR66385; ABR66385; MmarC7_1322.
DR GeneID; 5329467; -.
DR KEGG; mmz:MmarC7_1322; -.
DR eggNOG; arCOG01025; Archaea.
DR HOGENOM; CLU_073768_0_0_2; -.
DR OMA; WDVLVWT; -.
DR OrthoDB; 98200at2157; -.
DR UniPathway; UPA00053; UER00088.
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 Gene3D; 3.30.70.890; -; 1.
DR HAMAP; MF_00370; Shik_kinase_arch; 1.
DR InterPro; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
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; PF08544; GHMP_kinases_C; 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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; ATP-binding;
KW Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..283
FT /note="Shikimate kinase"
FT /id="PRO_1000059935"
FT BINDING 86..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00370"
SQ SEQUENCE 283 AA; 30330 MW; 6AC4FB5B41D44C73 CRC64;
MRCSAVSLGS GTIINAIATG FGSAFGVDLK IKADVELLDN GKKIINGISI DNPTLKPSLV
ERCVKNVLDY FEVDYSAKIS TSGDIPVKSG LSSSSAASNA AVLATIGALG EKVDSDLVLD
LAIKSSFEEK LTVTGAYDDA TASYFGGITV CNNMERKILK KDEFKEDIKV VVLMPEFQKN
VDVKRMKLIK DYVDMAFEKC MAGDYYKALF LNGLLYSSAL NFPSNISVDA LEAGAITAGL
SGTGPSYVAL CYNENEKNVE NALKKYGNTV ITKPCINGAR ILY