AROK_HALS3
ID AROK_HALS3 Reviewed; 284 AA.
AC B0R569;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=OE_2785R;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
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; AM774415; CAP13885.1; -; Genomic_DNA.
DR RefSeq; WP_010902901.1; NC_010364.1.
DR AlphaFoldDB; B0R569; -.
DR SMR; B0R569; -.
DR EnsemblBacteria; CAP13885; CAP13885; OE_2785R.
DR GeneID; 5954102; -.
DR KEGG; hsl:OE_2785R; -.
DR HOGENOM; CLU_073768_0_0_2; -.
DR OMA; WDVLVWT; -.
DR PhylomeDB; B0R569; -.
DR UniPathway; UPA00053; UER00088.
DR Proteomes; UP000001321; 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; 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 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..284
FT /note="Shikimate kinase"
FT /id="PRO_1000121518"
FT BINDING 85..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00370"
SQ SEQUENCE 284 AA; 28646 MW; F14CD2A7152E6C68 CRC64;
MDGRAVAPAA GTVLNALATG VGAAFALDID TEASVSVTPS ESGVSGEIAG HPEADTALVE
RCVSRVIDRY GDGQGGHVRT ESEVPLAAGL KSSSAAANAT VLATLDALGV ADEVDRVDAA
RLGVQAARDA GVTVTGAFDD AAASMLGGVA MTDNREDDLL FRDAVEWHAA VWTPPERAYS
ADADVARCER VSGLAEHVAA LAAAGDYGTA MTVNGLAFCA ALDFPTAPAV TALPHAAGVS
LSGTGPSYVA VGDEDGIEEV STRWHENPGT VRETTTQLAG ARTT
