ID U2R1L6_9ACTN Unreviewed; 562 AA.
AC U2R1L6;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 55.
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=aroB_1 {ECO:0000313|EMBL:ERK62404.1};
GN Synonyms=aroK {ECO:0000256|HAMAP-Rule:MF_00109};
GN ORFNames=HMPREF0682_2926 {ECO:0000313|EMBL:ERK62404.1};
OS Propionibacterium acidifaciens F0233.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionibacterium.
OX NCBI_TaxID=553198 {ECO:0000313|EMBL:ERK62404.1, ECO:0000313|Proteomes:UP000017052};
RN [1] {ECO:0000313|EMBL:ERK62404.1, ECO:0000313|Proteomes:UP000017052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0233 {ECO:0000313|EMBL:ERK62404.1,
RC ECO:0000313|Proteomes:UP000017052};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (AUG-2013) 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=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-
CC dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001393};
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 -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 2/7. {ECO:0000256|ARBA:ARBA00004661}.
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: 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:ERK62404.1}.
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DR EMBL; ACVN02000030; ERK62404.1; -; Genomic_DNA.
DR AlphaFoldDB; U2R1L6; -.
DR OrthoDB; 9806583at2; -.
DR UniPathway; UPA00053; UER00088.
DR Proteomes; UP000017052; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:InterPro.
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; cd08195; DHQS; 1.
DR CDD; cd00464; SK; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00109; Shikimate_kinase; 1.
DR InterPro; IPR016037; DHQ_synth_AroB.
DR InterPro; IPR030960; DHQS/DOIS.
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 NCBIfam; TIGR01357; aroB; 1.
DR PANTHER; PTHR43622; 3-DEHYDROQUINATE SYNTHASE; 1.
DR PANTHER; PTHR43622:SF7; 3-DEHYDROQUINATE SYNTHASE, CHLOROPLASTIC; 1.
DR Pfam; PF01761; DHQ_synthase; 1.
DR Pfam; PF01202; SKI; 1.
DR PRINTS; PR01100; SHIKIMTKNASE.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00109};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00109};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ERK62404.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00109};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00109};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
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 DOMAIN 270..525
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
FT BINDING 29..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 33
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
SQ SEQUENCE 562 AA; 60464 MW; EE48C6FFD2BDBCE4 CRC64;
MVDQPSAPGP DEPDEQEHRP AVVLVGPPGA GKTTVGTLIA HALGLPFLDT DDEVERVAGM
PIPEIFLTKG EPAFRALEHE TVLRVLREFD GIVALGGGAI LHPGTQEALR RHMTVFLDVD
VSQALPRVGL SGIRPLLMGD PVTKFNALMA QRRAIYESVS QIRLNTTGRR PQDSGEDILL
ALINAGTVDL PPGTVRRAAS RHAPASVVSV TGHDGYEIRI GWDLLPEAGE LIPRDAERVL
VAHEAVVAPS ADRLAEALEA GGRRVVRHEL PDPARTKSLD AVARLWDLLG EHRFGRRDAI
VAVGGAEAIY LLGFVGATWL RGVPVVNVPT SLLAMVDASV GGKAALDLPR GRDLVGAFHS
PCGVLCDLGL LASLPAEQLR SGLAEIVKAG FVGDEQILRL IEANGGADAL DIHSPVFREL
MERALAVKAR VVAEDLREVG LREILNYGHT LGHAIESCEG PAMRHGDAVA IGMVYAAELA
HRLGRLDAED LARHRSVLRM VGLPTGYSGA SWRQLSQAMS WDKKVRNDEL RFVVLEGIAK
CTIARAPDER LLRESWAAIR DR
//
