ID A0A174B533_9FIRM Unreviewed; 262 AA.
AC A0A174B533;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Shikimate kinase {ECO:0000256|HAMAP-Rule:MF_00109};
DE Short=SK {ECO:0000256|HAMAP-Rule:MF_00109};
DE EC=2.7.1.71 {ECO:0000256|HAMAP-Rule:MF_00109};
GN Name=aroK_2 {ECO:0000313|EMBL:CUN96211.1};
GN Synonyms=aroK {ECO:0000256|HAMAP-Rule:MF_00109};
GN ORFNames=DW021_01600 {ECO:0000313|EMBL:RHL50386.1}, DW222_04715
GN {ECO:0000313|EMBL:RHH20098.1}, DW272_05100
GN {ECO:0000313|EMBL:RHG18666.1}, DW723_00615
GN {ECO:0000313|EMBL:RHE78514.1}, DW767_01170
GN {ECO:0000313|EMBL:RHE15794.1}, DWX77_07845
GN {ECO:0000313|EMBL:RGS74258.1}, DWY46_01495
GN {ECO:0000313|EMBL:RGR51315.1}, DXB81_06535
GN {ECO:0000313|EMBL:RGN05670.1}, ERS852394_01234
GN {ECO:0000313|EMBL:CUN96211.1};
OS Blautia obeum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=40520 {ECO:0000313|EMBL:CUN96211.1, ECO:0000313|Proteomes:UP000095409};
RN [1] {ECO:0000313|EMBL:CUN96211.1, ECO:0000313|Proteomes:UP000095409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5608837 {ECO:0000313|EMBL:CUN96211.1,
RC ECO:0000313|Proteomes:UP000095409};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000261222, ECO:0000313|Proteomes:UP000283928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF21-24 {ECO:0000313|EMBL:RGS74258.1,
RC ECO:0000313|Proteomes:UP000284242}, AF25-21
RC {ECO:0000313|EMBL:RGR51315.1, ECO:0000313|Proteomes:UP000285839},
RC AF37-6AC {ECO:0000313|EMBL:RHL50386.1,
RC ECO:0000313|Proteomes:UP000285897}, AM18-2AC
RC {ECO:0000313|EMBL:RHH20098.1, ECO:0000313|Proteomes:UP000284024},
RC AM22-9LB {ECO:0000313|EMBL:RHG18666.1,
RC ECO:0000313|Proteomes:UP000284220}, AM27-32LB
RC {ECO:0000313|EMBL:RHE78514.1, ECO:0000313|Proteomes:UP000283928},
RC AM29-25AC {ECO:0000313|EMBL:RHE15794.1,
RC ECO:0000313|Proteomes:UP000284644}, and OM06-11AA
RC {ECO:0000313|EMBL:RGN05670.1, ECO:0000313|Proteomes:UP000261222};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-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_00109}.
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|HAMAP-Rule:MF_00109};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00109};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00109};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 5/7. {ECO:0000256|HAMAP-Rule:MF_00109}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00109}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00109}.
CC -!- SIMILARITY: Belongs to the shikimate kinase family. {ECO:0000256|HAMAP-
CC Rule:MF_00109}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00109}.
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DR EMBL; CYZD01000004; CUN96211.1; -; Genomic_DNA.
DR EMBL; QSUB01000002; RGN05670.1; -; Genomic_DNA.
DR EMBL; QRUH01000001; RGR51315.1; -; Genomic_DNA.
DR EMBL; QRVV01000017; RGS74258.1; -; Genomic_DNA.
DR EMBL; QSJW01000001; RHE15794.1; -; Genomic_DNA.
DR EMBL; QSKO01000001; RHE78514.1; -; Genomic_DNA.
DR EMBL; QRHZ01000002; RHG18666.1; -; Genomic_DNA.
DR EMBL; QRJH01000002; RHH20098.1; -; Genomic_DNA.
DR EMBL; QROS01000001; RHL50386.1; -; Genomic_DNA.
DR RefSeq; WP_022389105.1; NZ_QSUB01000002.1.
DR AlphaFoldDB; A0A174B533; -.
DR UniPathway; UPA00053; UER00088.
DR Proteomes; UP000095409; Unassembled WGS sequence.
DR Proteomes; UP000261222; Unassembled WGS sequence.
DR Proteomes; UP000283928; Unassembled WGS sequence.
DR Proteomes; UP000284024; Unassembled WGS sequence.
DR Proteomes; UP000284220; Unassembled WGS sequence.
DR Proteomes; UP000284242; Unassembled WGS sequence.
DR Proteomes; UP000284644; Unassembled WGS sequence.
DR Proteomes; UP000285839; Unassembled WGS sequence.
DR Proteomes; UP000285897; 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:0004106; F:chorismate mutase activity; IEA:UniProt.
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; 1.20.59.10; Chorismate mutase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00109; Shikimate_kinase; 1.
DR InterPro; IPR036263; Chorismate_II_sf.
DR InterPro; IPR036979; CM_dom_sf.
DR InterPro; IPR002701; CM_II_prokaryot.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR031322; Shikimate/glucono_kinase.
DR InterPro; IPR000623; Shikimate_kinase/TSH1.
DR PANTHER; PTHR21087; SHIKIMATE KINASE; 1.
DR PANTHER; PTHR21087:SF16; SHIKIMATE KINASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF01817; CM_2; 1.
DR Pfam; PF01202; SKI; 1.
DR PRINTS; PR01100; SHIKIMTKNASE.
DR SMART; SM00830; CM_2; 1.
DR SUPFAM; SSF48600; Chorismate mutase II; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51168; CHORISMATE_MUT_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00109};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_00109};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00109}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00109};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00109};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00109};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00109};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00109}; Reference proteome {ECO:0000313|Proteomes:UP000095409};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00109}.
FT DOMAIN 1..88
FT /note="Chorismate mutase"
FT /evidence="ECO:0000259|PROSITE:PS51168"
FT BINDING 100..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 104
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
SQ SEQUENCE 262 AA; 30316 MW; 6BAEE793C10BF284 CRC64;
MNQLEVLRES LGQCDEIVLD ALLMRNRIVE DIMAYKEAND IPILQPEQEA KQREWLNRRM
EGRRHKDEVT AVFEEITRNS KRIQARKLFD YNIVLIGFMG AGKSTISDFL KTVFAMEVVE
MDQIIAEREG MSISDIFETY GEEYFRNLET ELLIEMQSKT NVVISCGGGV PMRERNVVEM
KKNGRVVLLT AKPETILSRV KDNHDRPLLE GNKNVDFIAD LMEKRREKYQ AAADIVIETD
GKDKLEICEE LVQRIRALDA EE
//
