ID A5V1X1_ROSS1 Unreviewed; 176 AA.
AC A5V1X1;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Shikimate kinase {ECO:0000256|ARBA:ARBA00012154, ECO:0000256|HAMAP-Rule:MF_00109};
DE Short=SK {ECO:0000256|HAMAP-Rule:MF_00109};
DE EC=2.7.1.71 {ECO:0000256|ARBA:ARBA00012154, ECO:0000256|HAMAP-Rule:MF_00109};
GN Name=aroK {ECO:0000256|HAMAP-Rule:MF_00109};
GN OrderedLocusNames=RoseRS_4543 {ECO:0000313|EMBL:ABQ92874.1};
OS Roseiflexus sp. (strain RS-1).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Roseiflexus.
OX NCBI_TaxID=357808 {ECO:0000313|EMBL:ABQ92874.1, ECO:0000313|Proteomes:UP000006554};
RN [1] {ECO:0000313|Proteomes:UP000006554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS-1 {ECO:0000313|Proteomes:UP000006554};
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., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Bryant D.A., Richardson P.;
RT "Complete sequence of Roseiflexus sp. RS-1.";
RL Submitted (APR-2007) 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|ARBA:ARBA00000172,
CC 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|ARBA:ARBA00004842, 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; CP000686; ABQ92874.1; -; Genomic_DNA.
DR RefSeq; WP_011959211.1; NC_009523.1.
DR AlphaFoldDB; A5V1X1; -.
DR STRING; 357808.RoseRS_4543; -.
DR KEGG; rrs:RoseRS_4543; -.
DR eggNOG; COG0703; Bacteria.
DR HOGENOM; CLU_057607_2_3_0; -.
DR OrthoDB; 9800332at2; -.
DR UniPathway; UPA00053; UER00088.
DR Proteomes; UP000006554; Chromosome.
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 InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR031322; Shikimate/glucono_kinase.
DR InterPro; IPR000623; Shikimate_kinase/TSH1.
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_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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00109}.
FT BINDING 15..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 19
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 37
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 61
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
SQ SEQUENCE 176 AA; 18946 MW; 8576AF9A22F08755 CRC64;
MTGIPERIAL VGLSGSGKST VARLLAGRLG WHMCDTDAMV EQMTGRSIPA LFAEEGEAAF
RECESAALAA ALARTPVVIA TGGGIVVRES NRVLLKDQAL VVWLDAPTAV LIARLRTHEE
ERPLLAGDDP AVRLEALRAA RLPFYRQVAH LILDTSQMSP LQVAERIIAV VTRTEN
//
