GenomeNet

Database: UniProt
Entry: A0A1I6H5U5_9FLAO
LinkDB: A0A1I6H5U5_9FLAO
Original site: A0A1I6H5U5_9FLAO 
ID   A0A1I6H5U5_9FLAO        Unreviewed;       179 AA.
AC   A0A1I6H5U5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
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=SAMN04490243_2302 {ECO:0000313|EMBL:SFR49798.1};
OS   Robiginitalea myxolifaciens.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Robiginitalea.
OX   NCBI_TaxID=400055 {ECO:0000313|EMBL:SFR49798.1, ECO:0000313|Proteomes:UP000199534};
RN   [1] {ECO:0000313|EMBL:SFR49798.1, ECO:0000313|Proteomes:UP000199534}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21019 {ECO:0000313|EMBL:SFR49798.1,
RC   ECO:0000313|Proteomes:UP000199534};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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   ---------------------------------------------------------------------------
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; FOYQ01000002; SFR49798.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6H5U5; -.
DR   STRING; 400055.SAMN04490243_2302; -.
DR   OrthoDB; 9800332at2; -.
DR   UniPathway; UPA00053; UER00088.
DR   Proteomes; UP000199534; 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:SFR49798.1};
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:UP000199534};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00109}.
FT   BINDING         10..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT   BINDING         14
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT   BINDING         32
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT   BINDING         79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT   BINDING         119
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"
FT   BINDING         157
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
SQ   SEQUENCE   179 AA;  20270 MW;  12254C5261774579 CRC64;
     MQIVLVGYMG SGKSAVGRVL AEATGLDFTD LDNYIESREA LSIPQIFEQR GELYFRKREH
     ELLKEFLEQH QTGILALGGG TPCYAGNMDL LLGQTPHVFY LQLGVGQLVK RLEPEQQGRP
     LIAHLDKEEL PEFIGKHLFE RNPFYDKAHH VIRIQEQSAE EVVQQILTIL SAKTKQAED
//
DBGET integrated database retrieval system