ID A0A0U0WL44_SALET Unreviewed; 181 AA.
AC A0A0U0WL44;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Shikimate kinase 2 {ECO:0000256|HAMAP-Rule:MF_01269};
DE Short=SK 2 {ECO:0000256|HAMAP-Rule:MF_01269};
DE EC=2.7.1.71 {ECO:0000256|HAMAP-Rule:MF_01269};
GN Name=aroL {ECO:0000256|HAMAP-Rule:MF_01269,
GN ECO:0000313|EMBL:SUE48563.1};
GN ORFNames=B7N00_14825 {ECO:0000313|EMBL:EDG5018219.1}, B7N01_03730
GN {ECO:0000313|EMBL:EDG4993537.1}, B7N35_01725
GN {ECO:0000313|EMBL:EDG5124751.1}, B7N72_05420
GN {ECO:0000313|EMBL:EDG5369548.1}, B7N78_04750
GN {ECO:0000313|EMBL:EDG5279087.1}, B7N80_05825
GN {ECO:0000313|EMBL:EDG5287903.1}, B7N84_07980
GN {ECO:0000313|EMBL:EDG5266276.1}, DRU31_03810
GN {ECO:0000313|EMBL:EBS2451458.1}, E0916_06595
GN {ECO:0000313|EMBL:ECF1445630.1}, EJV93_07440
GN {ECO:0000313|EMBL:ECA2721042.1}, EWC73_07350
GN {ECO:0000313|EMBL:ECE8536031.1}, G0B02_02210
GN {ECO:0000313|EMBL:HAC6377952.1}, G0D18_05635
GN {ECO:0000313|EMBL:HAC6680155.1}, G2206_06585
GN {ECO:0000313|EMBL:HAE0434442.1}, NCTC5754_03522
GN {ECO:0000313|EMBL:SUE48563.1};
OS Salmonella enterica subsp. enterica serovar Bovismorbificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=58097 {ECO:0000313|EMBL:SUE48563.1, ECO:0000313|Proteomes:UP000254190};
RN [1] {ECO:0000313|EMBL:HAC6377952.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6377952.1}, M123
RC {ECO:0000313|EMBL:HAC6680155.1}, and MS140073
RC {ECO:0000313|EMBL:HAE0434442.1};
RX PubMed=30286803;
RA Souvorov A., Agarwala R., Lipman D.J.;
RT "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL Genome Biol. 19:153-153(2018).
RN [2] {ECO:0000313|EMBL:SUE48563.1, ECO:0000313|Proteomes:UP000254190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC5754 {ECO:0000313|EMBL:SUE48563.1,
RC ECO:0000313|Proteomes:UP000254190};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:HAC6680155.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6377952.1}, M123
RC {ECO:0000313|EMBL:HAC6680155.1}, and MS140073
RC {ECO:0000313|EMBL:HAE0434442.1};
RG NCBI Pathogen Detection Project;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:EBS2451458.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=136768 {ECO:0000313|EMBL:EDG4993537.1}, 138330
RC {ECO:0000313|EMBL:EDG5287903.1}, 143652
RC {ECO:0000313|EMBL:EDG5369548.1}, 273631
RC {ECO:0000313|EMBL:EDG5018219.1}, 330535
RC {ECO:0000313|EMBL:EDG5266276.1}, 333944
RC {ECO:0000313|EMBL:EDG5279087.1}, 337042
RC {ECO:0000313|EMBL:EDG5124751.1}, 387147
RC {ECO:0000313|EMBL:EBS2451458.1}, 470200
RC {ECO:0000313|EMBL:ECE8536031.1}, 598023
RC {ECO:0000313|EMBL:ECA2721042.1}, and 692616
RC {ECO:0000313|EMBL:ECF1445630.1};
RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl
CC group of shikimic acid using ATP as a cosubstrate. {ECO:0000256|HAMAP-
CC Rule:MF_01269}.
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:0000256|ARBA:ARBA00000172,
CC ECO:0000256|HAMAP-Rule:MF_01269};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01269};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01269};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 5/7. {ECO:0000256|ARBA:ARBA00004842, ECO:0000256|HAMAP-Rule:MF_01269}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01269}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01269}.
CC -!- DOMAIN: The LID domain closes over the active site upon ATP binding.
CC {ECO:0000256|HAMAP-Rule:MF_01269}.
CC -!- SIMILARITY: Belongs to the shikimate kinase family. AroL subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01269}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01269}.
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DR EMBL; AAGUWJ010000002; EBS2451458.1; -; Genomic_DNA.
DR EMBL; AAHTVM010000003; ECA2721042.1; -; Genomic_DNA.
DR EMBL; AAIJHK010000005; ECE8536031.1; -; Genomic_DNA.
DR EMBL; AAIKGE010000003; ECF1445630.1; -; Genomic_DNA.
DR EMBL; AAMEJW010000002; EDG4993537.1; -; Genomic_DNA.
DR EMBL; AAMEJY010000009; EDG5018219.1; -; Genomic_DNA.
DR EMBL; AAMEKY010000001; EDG5124751.1; -; Genomic_DNA.
DR EMBL; AAMEMC010000003; EDG5266276.1; -; Genomic_DNA.
DR EMBL; AAMEMH010000002; EDG5279087.1; -; Genomic_DNA.
DR EMBL; AAMEML010000004; EDG5287903.1; -; Genomic_DNA.
DR EMBL; AAMEMP010000003; EDG5369548.1; -; Genomic_DNA.
DR EMBL; DAAMEZ010000001; HAC6377952.1; -; Genomic_DNA.
DR EMBL; DAAMHM010000003; HAC6680155.1; -; Genomic_DNA.
DR EMBL; DAAQQK010000005; HAE0434442.1; -; Genomic_DNA.
DR EMBL; UGVQ01000002; SUE48563.1; -; Genomic_DNA.
DR RefSeq; WP_000983569.1; NZ_WFIN01000003.1.
DR AlphaFoldDB; A0A0U0WL44; -.
DR SMR; A0A0U0WL44; -.
DR UniPathway; UPA00053; UER00088.
DR Proteomes; UP000254190; Unassembled WGS sequence.
DR Proteomes; UP000839929; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00464; SK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00109; Shikimate_kinase; 1.
DR HAMAP; MF_01269; Shikimate_kinase_2; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR031322; Shikimate/glucono_kinase.
DR InterPro; IPR000623; Shikimate_kinase/TSH1.
DR InterPro; IPR027544; Shikimate_kinase_2.
DR InterPro; IPR023000; Shikimate_kinase_CS.
DR PANTHER; PTHR21087; SHIKIMATE KINASE; 1.
DR PANTHER; PTHR21087:SF16; SHIKIMATE KINASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF01202; SKI; 1.
DR PRINTS; PR01100; SHIKIMTKNASE.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS01128; SHIKIMATE_KINASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01269};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_01269};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01269}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01269};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01269};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01269};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01269};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01269};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01269}.
FT REGION 112..126
FT /note="LID domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01269"
FT BINDING 12..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01269"
FT BINDING 16
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01269"
FT BINDING 32
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01269"
FT BINDING 34
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01269"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01269"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01269"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01269"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01269"
SQ SEQUENCE 181 AA; 19804 MW; F2C4B2C36445C54C CRC64;
MMQPLYLVGP RGCGKTTIGM ALAQATGFRF ADTDRWLQSH VQMSVADIVE KEGWGGFRAR
ETAALEAVSA PSTVVATGGG IILTEYNRRY MHRVGVVIYL CAPVSTLVNR LEAEPEADLR
PTLTGKPLSE EVREVLEQRD ALYRETAHYI IDATKAPAQV VSEIIAALPP STQRLQGDVY
T
//
