GenomeNet

Database: UniProt
Entry: A0A0D6THH0_9RHOB
LinkDB: A0A0D6THH0_9RHOB
Original site: A0A0D6THH0_9RHOB 
ID   A0A0D6THH0_9RHOB        Unreviewed;       179 AA.
AC   A0A0D6THH0;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
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 {ECO:0000256|HAMAP-Rule:MF_00109};
GN   ORFNames=SY26_04750 {ECO:0000313|EMBL:KIX19596.1};
OS   Paracoccus sp. 228.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1192054 {ECO:0000313|EMBL:KIX19596.1, ECO:0000313|Proteomes:UP000032743};
RN   [1] {ECO:0000313|EMBL:KIX19596.1, ECO:0000313|Proteomes:UP000032743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=361 {ECO:0000313|EMBL:KIX19596.1,
RC   ECO:0000313|Proteomes:UP000032743};
RA   Karczewska-Golec J., Kochanowska-Lyzen M., Balut M., Golec P.,
RA   Madanecki P., Markert S., Piotrowski A., Schweder T., Szalewska-Palasz A.;
RT   "Three Bacterial Inhabitants of the Baltic Sea under Osmotic Stress: a
RT   Genomic and a Proteomic Perspective.";
RL   Submitted (FEB-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KIX19596.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JYGY01000001; KIX19596.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D6THH0; -.
DR   STRING; 1192054.SY26_04750; -.
DR   PATRIC; fig|1603292.4.peg.973; -.
DR   UniPathway; UPA00053; UER00088.
DR   Proteomes; UP000032743; 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   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; 1.
DR   Pfam; PF01202; SKI; 1.
DR   PRINTS; PR01100; SHIKIMTKNASE.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00109};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00109};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00109};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00109};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00109, ECO:0000313|EMBL:KIX19596.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00109};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00109};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00109};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032743};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00109}.
FT   BINDING         12..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT   BINDING         16
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT   BINDING         34
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT   BINDING         58
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT   BINDING         80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT   BINDING         118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
SQ   SEQUENCE   179 AA;  19434 MW;  FE6360D461FE7BF4 CRC64;
     MTRHIVLIGM MGAGKTAIGS ELARRLRVPF TDSDAEIEAA AAMSISEIFA RDGEAFFRAR
     EAQVLSRLLA GAPGVVSTGG GAWMRPENRQ IIGERGLSVW LNCSPETLWA RVRQRPTRPL
     LQTADPKGTL QRLLAERSPV YALADLEFVS RAGDTIEATA TRLIAELTAA HPTLTQEKP
//
DBGET integrated database retrieval system