ID E6SM12_THEM7 Unreviewed; 660 AA.
AC E6SM12;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00109, ECO:0000256|HAMAP-Rule:MF_00110};
DE Includes:
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};
DE Includes:
DE RecName: Full=3-dehydroquinate synthase {ECO:0000256|HAMAP-Rule:MF_00110};
DE Short=DHQS {ECO:0000256|HAMAP-Rule:MF_00110};
DE EC=4.2.3.4 {ECO:0000256|HAMAP-Rule:MF_00110};
GN Name=aroK {ECO:0000256|HAMAP-Rule:MF_00109};
GN Synonyms=aroB {ECO:0000256|HAMAP-Rule:MF_00110};
GN OrderedLocusNames=Tmar_0217 {ECO:0000313|EMBL:ADU50342.1};
OS Thermaerobacter marianensis (strain ATCC 700841 / DSM 12885 / JCM 10246 /
OS 7p75a).
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Clostridiales Family XVII. Incertae Sedis; Thermaerobacter.
OX NCBI_TaxID=644966 {ECO:0000313|EMBL:ADU50342.1, ECO:0000313|Proteomes:UP000008915};
RN [1] {ECO:0000313|EMBL:ADU50342.1, ECO:0000313|Proteomes:UP000008915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a
RC {ECO:0000313|Proteomes:UP000008915};
RX PubMed=21304738;
RA Han C., Gu W., Zhang X., Lapidus A., Nolan M., Copeland A., Lucas S.,
RA Del Rio T.G., Tice H., Cheng J.F., Tapia R., Goodwin L., Pitluck S.,
RA Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Schneider S., Rohde M., Goker M., Pukall R., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Detter J.C.;
RT "Complete genome sequence of Thermaerobacter marianensis type strain
RT (7p75a).";
RL Stand. Genomic Sci. 3:337-345(2010).
RN [2] {ECO:0000313|Proteomes:UP000008915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a
RC {ECO:0000313|Proteomes:UP000008915};
RX DOI=10.4056/sigs.1373474;
RA Han C., Gu W., Zhang X., Lapidus A., Nolan M., Copeland A., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J., Tapia R., Goodwin L., Pitluck S.,
RA Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Schneider S.,
RA Rohde M., Goker M., Pukall R., Woyke T., Bristow J., Eisen J.,
RA Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Detter J.;
RT "Complete genome sequence of Thermaerobacter marianensis type strain
RT (7p75aT).";
RL Stand. Genomic Sci. 3:337-345(2010).
CC -!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate
CC 7-phosphate (DAHP) to dehydroquinate (DHQ). {ECO:0000256|HAMAP-
CC Rule:MF_00110}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00110};
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=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00110};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00110};
CC Note=Binds 1 divalent metal cation per subunit. Can use either Co(2+)
CC or Zn(2+). {ECO:0000256|HAMAP-Rule:MF_00110};
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 ECO:0000256|HAMAP-Rule:MF_00110};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 2/7. {ECO:0000256|ARBA:ARBA00004661, ECO:0000256|HAMAP-Rule:MF_00110}.
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_00110}.
CC -!- SIMILARITY: Belongs to the shikimate kinase family. {ECO:0000256|HAMAP-
CC Rule:MF_00109}.
CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily.
CC Dehydroquinate synthase family. {ECO:0000256|HAMAP-Rule:MF_00110}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00110}.
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DR EMBL; CP002344; ADU50342.1; -; Genomic_DNA.
DR AlphaFoldDB; E6SM12; -.
DR STRING; 644966.Tmar_0217; -.
DR KEGG; tmr:Tmar_0217; -.
DR eggNOG; COG0337; Bacteria.
DR eggNOG; COG0703; Bacteria.
DR HOGENOM; CLU_001201_5_0_9; -.
DR UniPathway; UPA00053; UER00085.
DR Proteomes; UP000008915; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-UniRule.
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_00110; DHQ_synthase; 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_00110};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_00110};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00109}; Cobalt {ECO:0000256|HAMAP-Rule:MF_00110};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00110};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00109};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00110};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00109};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00110};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00110};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00110}; Reference proteome {ECO:0000313|Proteomes:UP000008915};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00109}; Zinc {ECO:0000256|HAMAP-Rule:MF_00110}.
FT DOMAIN 355..619
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
FT REGION 121..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 78
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 190
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109"
FT BINDING 392..396
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 416..417
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 429
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 438
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 456..459
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 471
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 534
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
FT BINDING 550
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00110"
SQ SEQUENCE 660 AA; 67531 MW; C342DCD9192F33B1 CRC64;
MRIVLVGLMG AGKTTVGRAL AARLGWAFLD LDDLIEQEAG QTVADLFARE GEAGFRTREE
QALATALTLE RVVLATGGGA VLSARNRQRL AAEPWVFWLE APPDELARRL AGPGAAARPL
LAGATGRPAT PPPAGSGAGF PAGSVGADVP NSGRSGEPGA HPARAGGAGG AGGPDAEALV
ARLAGLLQQR QAAYAAVARH RIPTAGRSVD QVVTGLLETL QASGWARPVQ GPSTRPYPAP
VPDPDLVIEA GPDRYPLWVR PGTVGPVEAA GLEVLVAAVA GLQSGGGGAG PAGSSGMVAR
SRGGGQPPAS GLAPPEPGER APVALLVSDP VVAALYGHGV AAALDQAGFH VVRAVVPAGE
EAKSLHWASA LYDRLLEAGA GRDAWVFALG GGVVGDLAGF VAATYMRGIA FAQLPTTLLA
QVDASAGGKV AVNHPRAKNL IGAFHQPRLV VADPATLVTQ PWPAYRGGLA EMVKHALLDG
EDHLASLEAA VPRLRERDPH QLAPLIARSV AVKARIVAVD PEERGPRAFL NLGHTFAHAL
EAATGYRVPH GDAVAAGLAL ALALSERLGM IPAGLAARVQ HLLARLGLPV TLAEACRAWD
VPPPEAAAVL GRLLYDKKNR RGRVRFVLLG APGQVTLRDD VPPALVEELV RRSLAGGPPA
//
