ID H3KDR3_9BURK Unreviewed; 625 AA.
AC H3KDR3;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
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=HMPREF9440_00874 {ECO:0000313|EMBL:EHY31758.1};
OS Sutterella parvirubra YIT 11816.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Sutterella.
OX NCBI_TaxID=762967 {ECO:0000313|EMBL:EHY31758.1, ECO:0000313|Proteomes:UP000004956};
RN [1] {ECO:0000313|EMBL:EHY31758.1, ECO:0000313|Proteomes:UP000004956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 11816 {ECO:0000313|EMBL:EHY31758.1,
RC ECO:0000313|Proteomes:UP000004956};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2011) 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:EHY31758.1}.
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DR EMBL; AFBQ01000119; EHY31758.1; -; Genomic_DNA.
DR RefSeq; WP_008541589.1; NZ_JH604928.1.
DR AlphaFoldDB; H3KDR3; -.
DR STRING; 762967.HMPREF9440_00874; -.
DR PATRIC; fig|762967.3.peg.693; -.
DR HOGENOM; CLU_437371_0_0_4; -.
DR OrthoDB; 9776868at2; -.
DR UniPathway; UPA00053; UER00088.
DR Proteomes; UP000004956; 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:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:InterPro.
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; cd01065; NAD_bind_Shikimate_DH; 1.
DR CDD; cd00464; SK; 1.
DR Gene3D; 1.20.59.10; Chorismate mutase; 1.
DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00109; Shikimate_kinase; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR036263; Chorismate_II_sf.
DR InterPro; IPR036979; CM_dom_sf.
DR InterPro; IPR002701; CM_II_prokaryot.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR031322; Shikimate/glucono_kinase.
DR InterPro; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR022893; Shikimate_DH_fam.
DR InterPro; IPR000623; Shikimate_kinase/TSH1.
DR PANTHER; PTHR21089:SF1; BIFUNCTIONAL 3-DEHYDROQUINATE DEHYDRATASE_SHIKIMATE DEHYDROGENASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR21089; SHIKIMATE DEHYDROGENASE; 1.
DR Pfam; PF01817; CM_2; 1.
DR Pfam; PF08501; Shikimate_dh_N; 1.
DR Pfam; PF01202; SKI; 1.
DR PRINTS; PR01100; SHIKIMTKNASE.
DR SMART; SM00830; CM_2; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF48600; Chorismate mutase II; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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|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:EHY31758.1};
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000004956};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00109}.
FT DOMAIN 18..106
FT /note="Chorismate mutase"
FT /evidence="ECO:0000259|PROSITE:PS51168"
FT BINDING 475..480
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 479
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 497
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 521
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 543
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 576
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 591
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
SQ SEQUENCE 625 AA; 66781 MW; F1AB1DD23442357D CRC64;
MDQTVISVSH DEIRDPAAHA AKVIRRERVR IDAADRAILD AMRGRFEAVA AIGAAKRRAG
LPVYDAAREA ALYARISEMA GDLAPAALAL WRVMTAAARR MEGLDVRHEE ADRADQAAQS
ALPTTLTLEL PDAAMLTTVT TILAVHECVP AAMTWDGAAR RMTISVTEGS AWAPAMLSDL
TAQGVRIPEM EKVAEMAAEM TTGQAAEQSA PSRPRCGLLG RKLGYSYSPA IHAALGDYDY
DLHEVPNEED LEKFLKETPF DGLNVTIPYK VAVMAHCATL SPRAKAIGSV NTLVRRPDGT
LHGDNTDDAG FTAMVEESGV DPAGKTCVVL GSGGASRTVV AVLKRMGAKR VVVVSRRGED
HYGNLARHAD AALLVNATPV GMYPNVDASP VEDLSVFPKL EAVLDLIYNP PKTKLLADAE
KRGIRTVNGL RMLVVQAAVA SALWGCSAYD AKRCAAIEAA IRLGEENLWL VGMPGVGKTT
VGGLLGEALG RPFVDLDAEI ERVAGMPIPE IFRTRGEAGF REIEAEAAMT ASRGRGTVIA
TGGGTVLREA NRRAMRESGT VVWLQRDLSR LPTEGRPLSE AKGVEKLYAE REPIYRAAAH
LEVDANLLAG AEAVAEHVIG RLMRA
//
