AROD_SALTI
ID AROD_SALTI Reviewed; 252 AA.
AC P24670;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000303|PubMed:2045778};
DE Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000303|PubMed:2045778};
DE EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:24957267};
DE AltName: Full=Type I DHQase {ECO:0000255|HAMAP-Rule:MF_00214};
DE AltName: Full=Type I dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000303|PubMed:24957267};
DE Short=DHQ1 {ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000303|PubMed:24957267};
GN Name=aroD {ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000303|PubMed:2045778};
GN OrderedLocusNames=STY1760, t1231;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=2045778; DOI=10.1099/00221287-137-1-147;
RA Servos S., Chatfield S., Hone D., Levine M., Dimitriadis G., Pickard D.,
RA Dougan G., Fairweather N., Charles I.G.;
RT "Molecular cloning and characterization of the aroD gene encoding 3-
RT dehydroquinase from Salmonella typhi.";
RL J. Gen. Microbiol. 137:147-152(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH 3-DEHYDROQUINATE,
RP SUBUNIT, AND ACTIVE SITE.
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 [5]
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) IN COMPLEX WITH 3-DEHYDROSHIKIMATE,
RP ACTIVE SITE, AND SUBUNIT.
RX PubMed=11976491; DOI=10.1107/s0907444902003918;
RA Lee W.H., Perles L.A., Nagem R.A., Shrive A.K., Hawkins A., Sawyer L.,
RA Polikarpov I.;
RT "Comparison of different crystal forms of 3-dehydroquinase from Salmonella
RT typhi and its implication for the enzyme activity.";
RL Acta Crystallogr. D 58:798-804(2002).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND SUBUNIT.
RX PubMed=24957267; DOI=10.1042/bj20140614;
RA Maneiro M., Peon A., Lence E., Otero J.M., Van Raaij M.J., Thompson P.,
RA Hawkins A.R., Gonzalez-Bello C.;
RT "Insights into substrate binding and catalysis in bacterial type I
RT dehydroquinase.";
RL Biochem. J. 462:415-424(2014).
CC -!- FUNCTION: Involved in the third step of the chorismate pathway, which
CC leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-
CC dehydration of 3-dehydroquinate (DHQ) and introduces the first double
CC bond of the aromatic ring to yield 3-dehydroshikimate. The reaction
CC involves the formation of an imine intermediate between the keto group
CC of 3-dehydroquinate and the epsilon-amino group of Lys-170 at the
CC active site. {ECO:0000255|HAMAP-Rule:MF_00214,
CC ECO:0000269|PubMed:24957267}.
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_00214, ECO:0000269|PubMed:24957267};
CC -!- ACTIVITY REGULATION: Inhibited by (2R)-2-methyl-3-dehydroquinic acid.
CC {ECO:0000269|PubMed:24957267}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=24 uM for 3-dehydroquinate (at pH 7.2 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:24957267};
CC Note=kcat is 1.1 sec(-1) for dehydratase activity with 3-
CC dehydroquinate (at pH 7.2 and 25 degrees Celsius).
CC {ECO:0000269|PubMed:24957267};
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_00214}.
CC -!- SUBUNIT: Dimer of dimers. {ECO:0000255|HAMAP-Rule:MF_00214,
CC ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491,
CC ECO:0000269|PubMed:24957267}.
CC -!- SIMILARITY: Belongs to the type-I 3-dehydroquinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00214}.
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DR EMBL; X54546; CAA38418.1; -; Genomic_DNA.
DR EMBL; AL513382; CAD02002.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO68886.1; -; Genomic_DNA.
DR PIR; S15652; S15652.
DR RefSeq; NP_456161.1; NC_003198.1.
DR RefSeq; WP_000860215.1; NZ_WSUR01000011.1.
DR PDB; 1GQN; X-ray; 1.78 A; A=1-252.
DR PDB; 1L9W; X-ray; 2.10 A; A/B/C/D=1-252.
DR PDB; 1QFE; X-ray; 2.10 A; A/B=1-252.
DR PDB; 4CLM; X-ray; 1.40 A; A/B=1-252.
DR PDB; 4CNN; X-ray; 1.00 A; A/B=1-252.
DR PDB; 4CNO; X-ray; 1.50 A; A/B/C/D=1-252.
DR PDB; 4CNP; X-ray; 1.15 A; A/B=1-252.
DR PDB; 4UIO; X-ray; 1.35 A; A=1-252.
DR PDB; 6H5C; X-ray; 1.14 A; A/B=1-252.
DR PDB; 6H5D; X-ray; 1.25 A; A/B=1-252.
DR PDB; 6H5G; X-ray; 1.04 A; A=1-252.
DR PDB; 6H5J; X-ray; 1.40 A; A=1-252.
DR PDB; 6SFE; X-ray; 1.08 A; A/B=1-252.
DR PDB; 6SFG; X-ray; 1.23 A; A=1-252.
DR PDBsum; 1GQN; -.
DR PDBsum; 1L9W; -.
DR PDBsum; 1QFE; -.
DR PDBsum; 4CLM; -.
DR PDBsum; 4CNN; -.
DR PDBsum; 4CNO; -.
DR PDBsum; 4CNP; -.
DR PDBsum; 4UIO; -.
DR PDBsum; 6H5C; -.
DR PDBsum; 6H5D; -.
DR PDBsum; 6H5G; -.
DR PDBsum; 6H5J; -.
DR PDBsum; 6SFE; -.
DR PDBsum; 6SFG; -.
DR AlphaFoldDB; P24670; -.
DR PCDDB; P24670; -.
DR SMR; P24670; -.
DR STRING; 220341.16502840; -.
DR DrugBank; DB03746; 3-Amino-4,5-Dihydroxy-Cyclohex-1-Enecarboxylate.
DR EnsemblBacteria; AAO68886; AAO68886; t1231.
DR KEGG; stt:t1231; -.
DR KEGG; sty:STY1760; -.
DR PATRIC; fig|220341.7.peg.1771; -.
DR eggNOG; COG0710; Bacteria.
DR HOGENOM; CLU_064444_0_0_6; -.
DR OMA; ATMAMGE; -.
DR BRENDA; 4.2.1.10; 5557.
DR SABIO-RK; P24670; -.
DR UniPathway; UPA00053; UER00086.
DR EvolutionaryTrace; P24670; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IDA:UniProtKB.
DR GO; GO:0046279; P:3,4-dihydroxybenzoate biosynthetic process; IDA:UniProtKB.
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; cd00502; DHQase_I; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00214; AroD; 1.
DR InterPro; IPR018508; 3-dehydroquinate_DH_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001381; DHquinase_I.
DR Pfam; PF01487; DHquinase_I; 1.
DR TIGRFAMs; TIGR01093; aroD; 1.
DR PROSITE; PS01028; DEHYDROQUINASE_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Lyase; Schiff base.
FT CHAIN 1..252
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_0000138805"
FT ACT_SITE 143
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214,
FT ECO:0000305|PubMed:24957267"
FT ACT_SITE 170
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214,
FT ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491"
FT BINDING 21
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214,
FT ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491"
FT BINDING 46..48
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214,
FT ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491,
FT ECO:0000269|PubMed:24957267"
FT BINDING 82
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214,
FT ECO:0000269|PubMed:10360352"
FT BINDING 213
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214,
FT ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491,
FT ECO:0000269|PubMed:24957267"
FT BINDING 232
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214,
FT ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491"
FT BINDING 236
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214,
FT ECO:0000269|PubMed:10360352, ECO:0000269|PubMed:11976491,
FT ECO:0000269|PubMed:24957267"
FT CONFLICT 156
FT /note="L -> S (in Ref. 1; CAA38418)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:4CNN"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:4CNN"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:4CNN"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:4CNN"
FT HELIX 27..36
FT /evidence="ECO:0007829|PDB:4CNN"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:4CNN"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:4CNN"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:4CNN"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:6H5C"
FT HELIX 58..71
FT /evidence="ECO:0007829|PDB:4CNN"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:6H5C"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:4CNN"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:4CNN"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:4CNN"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:4CNN"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:4CNN"
FT HELIX 121..133
FT /evidence="ECO:0007829|PDB:4CNN"
FT STRAND 137..146
FT /evidence="ECO:0007829|PDB:4CNN"
FT HELIX 151..163
FT /evidence="ECO:0007829|PDB:4CNN"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:4CNN"
FT HELIX 178..194
FT /evidence="ECO:0007829|PDB:4CNN"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:4CNN"
FT TURN 206..210
FT /evidence="ECO:0007829|PDB:4CNN"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:4CNN"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:4CNN"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:4CNN"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:6SFE"
FT HELIX 239..251
FT /evidence="ECO:0007829|PDB:4CNN"
SQ SEQUENCE 252 AA; 27649 MW; F9D4D4C86D18F17B CRC64;
MKTVTVKNLI IGEGMPKIIV SLMGRDINSV KAEALAYREA TFDILEWRVD HFMDIASTQS
VLTAARVIRD AMPDIPLLFT FRSAKEGGEQ TITTQHYLTL NRAAIDSGLV DMIDLELFTG
DADVKATVDY AHAHNVYVVM SNHDFHQTPS AEEMVLRLRK MQALGADIPK IAVMPQSKHD
VLTLLTATLE MQQHYADRPV ITMSMAKEGV ISRLAGEVFG SAATFGAVKQ ASAPGQIAVN
DLRSVLMILH NA
