AROQ_THET8
ID AROQ_THET8 Reviewed; 149 AA.
AC Q5SIL5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_00169};
DE Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00169};
DE EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_00169};
DE AltName: Full=Type II DHQase {ECO:0000255|HAMAP-Rule:MF_00169};
GN Name=aroQ {ECO:0000255|HAMAP-Rule:MF_00169}; OrderedLocusNames=TTHA1354;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate.
CC {ECO:0000255|HAMAP-Rule:MF_00169}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O;
CC Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
CC ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00169};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 3/7. {ECO:0000255|HAMAP-Rule:MF_00169}.
CC -!- SUBUNIT: Homododecamer. {ECO:0000255|HAMAP-Rule:MF_00169}.
CC -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00169}.
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DR EMBL; AP008226; BAD71177.1; -; Genomic_DNA.
DR RefSeq; WP_011173409.1; NC_006461.1.
DR RefSeq; YP_144620.1; NC_006461.1.
DR PDB; 2UYG; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-149.
DR PDBsum; 2UYG; -.
DR AlphaFoldDB; Q5SIL5; -.
DR SMR; Q5SIL5; -.
DR STRING; 300852.55772736; -.
DR EnsemblBacteria; BAD71177; BAD71177; BAD71177.
DR GeneID; 3169111; -.
DR KEGG; ttj:TTHA1354; -.
DR PATRIC; fig|300852.9.peg.1331; -.
DR eggNOG; COG0757; Bacteria.
DR HOGENOM; CLU_090968_3_0_0; -.
DR OMA; AYTHYSY; -.
DR PhylomeDB; Q5SIL5; -.
DR UniPathway; UPA00053; UER00086.
DR EvolutionaryTrace; Q5SIL5; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00466; DHQase_II; 1.
DR Gene3D; 3.40.50.9100; -; 1.
DR HAMAP; MF_00169; AroQ; 1.
DR InterPro; IPR001874; DHquinase_II.
DR InterPro; IPR018509; DHquinase_II_CS.
DR InterPro; IPR036441; DHquinase_II_sf.
DR PANTHER; PTHR21272; PTHR21272; 1.
DR Pfam; PF01220; DHquinase_II; 1.
DR PIRSF; PIRSF001399; DHquinase_II; 1.
DR SUPFAM; SSF52304; SSF52304; 1.
DR TIGRFAMs; TIGR01088; aroQ; 1.
DR PROSITE; PS01029; DEHYDROQUINASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Lyase; Reference proteome.
FT CHAIN 1..149
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_1000023528"
FT ACT_SITE 21
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT ACT_SITE 99
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 100..101
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT SITE 16
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:2UYG"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:2UYG"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:2UYG"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:2UYG"
FT HELIX 26..39
FT /evidence="ECO:0007829|PDB:2UYG"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:2UYG"
FT HELIX 52..61
FT /evidence="ECO:0007829|PDB:2UYG"
FT TURN 62..66
FT /evidence="ECO:0007829|PDB:2UYG"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:2UYG"
FT HELIX 75..79
FT /evidence="ECO:0007829|PDB:2UYG"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:2UYG"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:2UYG"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:2UYG"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:2UYG"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:2UYG"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:2UYG"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:2UYG"
SQ SEQUENCE 149 AA; 16454 MW; 8AF31B5900F7ABED CRC64;
MVLILNGPNL NLLGRREPEV YGRTTLEELE ALCEAWGAEL GLGVVFRQTN YEGQLIEWVQ
QAHQEGFLAI VLNPGALTHY SYALLDAIRA QPLPVVEVHL TNLHAREEFR RHSVTAPACR
GIVSGFGPLS YKLALVYLAE TLEVGGEGF
