AROK_METTP
ID AROK_METTP Reviewed; 288 AA.
AC A0B8V5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Mthe_1354;
OS Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 /
OS PT) (Methanosaeta thermophila).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=349307;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Smith K.S., Ingram-Smith C., Richardson P.;
RT "Complete sequence of Methanosaeta thermophila PT.";
RL Submitted (OCT-2006) 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; CP000477; ABK15129.1; -; Genomic_DNA.
DR AlphaFoldDB; A0B8V5; -.
DR SMR; A0B8V5; -.
DR STRING; 349307.Mthe_1354; -.
DR EnsemblBacteria; ABK15129; ABK15129; Mthe_1354.
DR KEGG; mtp:Mthe_1354; -.
DR HOGENOM; CLU_073768_0_0_2; -.
DR OMA; WDVLVWT; -.
DR UniPathway; UPA00053; UER00088.
DR Proteomes; UP000000674; 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; 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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; ATP-binding;
KW Cytoplasm; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..288
FT /note="Shikimate kinase"
FT /id="PRO_1000059938"
FT BINDING 81..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00370"
SQ SEQUENCE 288 AA; 30091 MW; 5278C0E0BCF221E7 CRC64;
MRGYATAYGA ATVLNAIANW KGSAFGISLR TSAEVVLDDS EGVRGDVEGI DTTLIVRCVE
SVLSHFDLDY GGVVRTRSEI PVASGLKSSS AAANAAVLAT VDALGEEIDM IDAVRIGVEA
ALDAGVTVTG AFDDACASML GGVVVTDNLK RCLLKRDELH SDVVLLIPEE QFFSRDVDVE
RCRALSRVAD AVFEMAIEGD YAGAMTLNGL LYCTALRRSP EPIVLALRAG AAGATLSGTG
PAYAALVDDI SGDDVVEAWS SLGGRIIRAA VENRSARMGQ ADLFQEGI