AROQ_MYCTU
ID AROQ_MYCTU Reviewed; 147 AA.
AC P9WPX7; L0TCT6; P0A4Z6; P36918; P95016;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=3-dehydroquinate dehydratase;
DE Short=3-dehydroquinase;
DE EC=4.2.1.10;
DE AltName: Full=Type II DHQase;
GN Name=aroQ; Synonyms=aroD; OrderedLocusNames=Rv2537c; ORFNames=MTCY159.19;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=1910148; DOI=10.1007/bf00260631;
RA Garbe T., Servos S., Hawkins A., Dimitriadis G., Young D., Dougan G.,
RA Charles I.G.;
RT "The Mycobacterium tuberculosis shikimate pathway genes: evolutionary
RT relationship between biosynthetic and catabolic 3-dehydroquinases.";
RL Mol. Gen. Genet. 228:385-392(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT.
RX PubMed=10360352; DOI=10.1038/9287;
RA Gourley D.G., Shrive A.K., Polikarpov I., Krell T., Coggins J.R.,
RA Hawkins A.R., Isaacs N.W., Sawyer L.;
RT "The two types of 3-dehydroquinase have distinct structures but catalyze
RT the same overall reaction.";
RL Nat. Struct. Biol. 6:521-525(1999).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH POLYANION.
RX PubMed=12387860; DOI=10.1016/s0014-5793(02)03346-x;
RA Evans L.D., Roszak A.W., Noble L.J., Robinson D.A., Chalk P.A.,
RA Matthews J.L., Coggins J.R., Price N.C., Lapthorn A.J.;
RT "Specificity of substrate recognition by type II dehydroquinases as
RT revealed by binding of polyanions.";
RL FEBS Lett. 530:24-30(2002).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS.
RA Robinson D.A., Roszak A.W., Frederickson M., Abell C., Coggins J.R.,
RA Lapthorn A.J.;
RT "Structural basis for specificity of oxime based inhibitors towards type II
RT dehydroquinase from Mycobacterium tuberculosis.";
RL Submitted (MAY-2004) to the PDB data bank.
CC -!- FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate.
CC {ECO:0000250}.
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;
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 3/7.
CC -!- SUBUNIT: Homododecamer. {ECO:0000269|PubMed:10360352,
CC ECO:0000269|PubMed:12387860, ECO:0000269|Ref.7}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
CC {ECO:0000305}.
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; X59509; CAA42096.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP45332.1; -; Genomic_DNA.
DR PIR; E70658; E70658.
DR RefSeq; NP_217053.1; NC_000962.3.
DR RefSeq; WP_003413001.1; NZ_NVQJ01000032.1.
DR PDB; 1H05; X-ray; 1.50 A; A=2-147.
DR PDB; 1H0R; X-ray; 2.10 A; A=2-147.
DR PDB; 1H0S; X-ray; 1.70 A; A=2-147.
DR PDB; 2DHQ; X-ray; 2.00 A; A=2-147.
DR PDB; 2XB8; X-ray; 2.40 A; A=2-147.
DR PDB; 2Y71; X-ray; 1.50 A; A=2-147.
DR PDB; 2Y76; X-ray; 2.50 A; A=2-147.
DR PDB; 2Y77; X-ray; 1.50 A; A=2-147.
DR PDB; 3N59; X-ray; 2.52 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-147.
DR PDB; 3N76; X-ray; 1.90 A; A=1-147.
DR PDB; 3N7A; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-147.
DR PDB; 3N86; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-147.
DR PDB; 3N87; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-147.
DR PDB; 3N8K; X-ray; 2.25 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-147.
DR PDB; 3N8N; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-147.
DR PDB; 4B6O; X-ray; 2.00 A; A=2-147.
DR PDB; 4B6P; X-ray; 2.30 A; A=2-147.
DR PDB; 4B6Q; X-ray; 1.54 A; A=2-147.
DR PDB; 4CIV; X-ray; 2.90 A; A=2-147.
DR PDB; 4CIW; X-ray; 2.20 A; A=2-147.
DR PDB; 4CIX; X-ray; 2.90 A; A=2-147.
DR PDB; 4CIY; X-ray; 2.10 A; A=2-147.
DR PDB; 4CKW; X-ray; 2.70 A; A/B/C/D=2-147.
DR PDB; 4CKX; X-ray; 2.60 A; A=2-147.
DR PDB; 4CKY; X-ray; 1.65 A; A=2-147.
DR PDB; 4CKZ; X-ray; 2.52 A; A/B=2-147.
DR PDB; 4CL0; X-ray; 3.10 A; A=2-147.
DR PDB; 4KI7; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-147.
DR PDB; 4KIJ; X-ray; 2.80 A; A=1-147.
DR PDB; 4KIU; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-147.
DR PDB; 4KIW; X-ray; 2.57 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-147.
DR PDB; 4V0S; X-ray; 1.55 A; A/B=2-147.
DR PDBsum; 1H05; -.
DR PDBsum; 1H0R; -.
DR PDBsum; 1H0S; -.
DR PDBsum; 2DHQ; -.
DR PDBsum; 2XB8; -.
DR PDBsum; 2Y71; -.
DR PDBsum; 2Y76; -.
DR PDBsum; 2Y77; -.
DR PDBsum; 3N59; -.
DR PDBsum; 3N76; -.
DR PDBsum; 3N7A; -.
DR PDBsum; 3N86; -.
DR PDBsum; 3N87; -.
DR PDBsum; 3N8K; -.
DR PDBsum; 3N8N; -.
DR PDBsum; 4B6O; -.
DR PDBsum; 4B6P; -.
DR PDBsum; 4B6Q; -.
DR PDBsum; 4CIV; -.
DR PDBsum; 4CIW; -.
DR PDBsum; 4CIX; -.
DR PDBsum; 4CIY; -.
DR PDBsum; 4CKW; -.
DR PDBsum; 4CKX; -.
DR PDBsum; 4CKY; -.
DR PDBsum; 4CKZ; -.
DR PDBsum; 4CL0; -.
DR PDBsum; 4KI7; -.
DR PDBsum; 4KIJ; -.
DR PDBsum; 4KIU; -.
DR PDBsum; 4KIW; -.
DR PDBsum; 4V0S; -.
DR AlphaFoldDB; P9WPX7; -.
DR SMR; P9WPX7; -.
DR STRING; 83332.Rv2537c; -.
DR BindingDB; P9WPX7; -.
DR ChEMBL; CHEMBL3345; -.
DR DrugBank; DB02801; 2,3-Anhydro-quinic acid.
DR DrugBank; DB03739; 3-Hydroxyimino Quinic Acid.
DR PaxDb; P9WPX7; -.
DR DNASU; 888397; -.
DR GeneID; 888397; -.
DR KEGG; mtu:Rv2537c; -.
DR TubercuList; Rv2537c; -.
DR eggNOG; COG0757; Bacteria.
DR OMA; AYTHYSY; -.
DR PhylomeDB; P9WPX7; -.
DR BRENDA; 4.2.1.10; 3445.
DR Reactome; R-MTU-964903; Chorismate via Shikimate Pathway.
DR UniPathway; UPA00053; UER00086.
DR PRO; PR:P9WPX7; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IDA:MTBBASE.
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 GO; GO:0019631; P:quinate catabolic process; IBA:GO_Central.
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..147
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_0000159910"
FT ACT_SITE 25
FT /note="Proton acceptor"
FT ACT_SITE 102
FT /note="Proton donor"
FT BINDING 76
FT /ligand="substrate"
FT BINDING 82
FT /ligand="substrate"
FT BINDING 89
FT /ligand="substrate"
FT BINDING 103..104
FT /ligand="substrate"
FT BINDING 113
FT /ligand="substrate"
FT SITE 20
FT /note="Transition state stabilizer"
FT CONFLICT 117
FT /note="Y -> I (in Ref. 1; CAA42096)"
FT /evidence="ECO:0000305"
FT TURN 1..3
FT /evidence="ECO:0007829|PDB:4KI7"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:1H05"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:1H05"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:1H05"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:2Y71"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:4CIY"
FT HELIX 30..43
FT /evidence="ECO:0007829|PDB:1H05"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:1H05"
FT HELIX 56..69
FT /evidence="ECO:0007829|PDB:1H05"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:1H05"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:1H05"
FT HELIX 85..92
FT /evidence="ECO:0007829|PDB:1H05"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:1H05"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:1H05"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:1H05"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1H05"
FT STRAND 122..129
FT /evidence="ECO:0007829|PDB:1H05"
FT HELIX 132..143
FT /evidence="ECO:0007829|PDB:1H05"
SQ SEQUENCE 147 AA; 15790 MW; 9EE0E1B14B4DB5F6 CRC64;
MSELIVNVIN GPNLGRLGRR EPAVYGGTTH DELVALIERE AAELGLKAVV RQSDSEAQLL
DWIHQAADAA EPVILNAGGL THTSVALRDA CAELSAPLIE VHISNVHARE EFRRHSYLSP
IATGVIVGLG IQGYLLALRY LAEHVGT
