AROK_PYRFU
ID AROK_PYRFU Reviewed; 273 AA.
AC Q8U0A5;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=PF1694;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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; AE009950; AAL81818.1; -; Genomic_DNA.
DR RefSeq; WP_011012840.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U0A5; -.
DR SMR; Q8U0A5; -.
DR STRING; 186497.PF1694; -.
DR EnsemblBacteria; AAL81818; AAL81818; PF1694.
DR GeneID; 41713525; -.
DR KEGG; pfu:PF1694; -.
DR PATRIC; fig|186497.12.peg.1762; -.
DR eggNOG; arCOG01025; Archaea.
DR HOGENOM; CLU_073768_0_0_2; -.
DR OMA; WDVLVWT; -.
DR OrthoDB; 98200at2157; -.
DR PhylomeDB; Q8U0A5; -.
DR UniPathway; UPA00053; UER00088.
DR Proteomes; UP000001013; 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..273
FT /note="Shikimate kinase"
FT /id="PRO_0000141578"
FT BINDING 85..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00370"
SQ SEQUENCE 273 AA; 29318 MW; 7551661EB76E09A7 CRC64;
MRGLGKGSSA ITVVNAFATG KGGAIGIDLW TEAKVKITDG EVKGKILVNG LEFNDFRVVN
AVLDVMRRYS GIEFGIEFEI NSEIPVGKGL KSSSAVANAL VEAIARALRL NIPGIKVVKL
GVEAAKKAGV TLTGAFDDAC ASYFGGLCLT DNLRVELLKR IEIDELPVVI LVPNETVLTE
ELKGVDFLKI APYVEEAFKL AIKGEWKKAL VLNGLIYSTF LSYPPEPISK ALHLGAVVGL
SGKGPSVFAI TDEPERIEEV WREFGDVIIT STR