AROD_AQUAE
ID AROD_AQUAE Reviewed; 219 AA.
AC O66440;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_00214};
DE Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00214};
DE EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_00214};
DE AltName: Full=Type I DHQase {ECO:0000255|HAMAP-Rule:MF_00214};
DE AltName: Full=Type I dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00214};
DE Short=DHQ1 {ECO:0000255|HAMAP-Rule:MF_00214};
GN Name=aroD {ECO:0000255|HAMAP-Rule:MF_00214}; OrderedLocusNames=aq_021;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP ACTIVE SITE, AND SUBUNIT.
RX PubMed=23396056; DOI=10.1016/j.bbrc.2013.01.099;
RA Devi A.S., Ebihara A., Kuramitsu S., Yokoyama S., Kumarevel T.S.,
RA Ponnuraj K.;
RT "Crystal structure of type I 3-dehydroquinate dehydratase of Aquifex
RT aeolicus suggests closing of active site flap is not essential for enzyme
RT action.";
RL Biochem. Biophys. Res. Commun. 432:350-354(2013).
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.
CC {ECO:0000255|HAMAP-Rule:MF_00214}.
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};
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: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00214,
CC ECO:0000269|PubMed:23396056}.
CC -!- SIMILARITY: Belongs to the type-I 3-dehydroquinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00214}.
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DR EMBL; AE000657; AAC06389.1; -; Genomic_DNA.
DR PIR; E70301; E70301.
DR RefSeq; NP_212999.1; NC_000918.1.
DR RefSeq; WP_010879937.1; NC_000918.1.
DR PDB; 2EGZ; X-ray; 1.75 A; A/C=1-219.
DR PDB; 2YSW; X-ray; 2.25 A; A/B/C=1-219.
DR PDBsum; 2EGZ; -.
DR PDBsum; 2YSW; -.
DR AlphaFoldDB; O66440; -.
DR SMR; O66440; -.
DR STRING; 224324.aq_021; -.
DR EnsemblBacteria; AAC06389; AAC06389; aq_021.
DR KEGG; aae:aq_021; -.
DR PATRIC; fig|224324.8.peg.14; -.
DR eggNOG; COG0710; Bacteria.
DR HOGENOM; CLU_064444_2_1_0; -.
DR InParanoid; O66440; -.
DR OMA; FATMSMG; -.
DR OrthoDB; 1298468at2; -.
DR UniPathway; UPA00053; UER00086.
DR EvolutionaryTrace; O66440; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IBA:GO_Central.
DR GO; GO:0046279; P:3,4-dihydroxybenzoate biosynthetic process; IBA:GO_Central.
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; Reference proteome; Schiff base.
FT CHAIN 1..219
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_0000138792"
FT ACT_SITE 116
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214,
FT ECO:0000269|PubMed:23396056"
FT ACT_SITE 142
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214,
FT ECO:0000269|PubMed:23396056"
FT BINDING 28..30
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 61
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214,
FT ECO:0000269|PubMed:23396056"
FT BINDING 180
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214,
FT ECO:0000269|PubMed:23396056"
FT BINDING 203
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2EGZ"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:2EGZ"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:2EGZ"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:2EGZ"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:2EGZ"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:2EGZ"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:2EGZ"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:2EGZ"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:2EGZ"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:2EGZ"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:2EGZ"
FT HELIX 97..106
FT /evidence="ECO:0007829|PDB:2EGZ"
FT STRAND 110..119
FT /evidence="ECO:0007829|PDB:2EGZ"
FT HELIX 124..136
FT /evidence="ECO:0007829|PDB:2EGZ"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:2EGZ"
FT HELIX 150..160
FT /evidence="ECO:0007829|PDB:2EGZ"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:2EGZ"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:2EGZ"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:2EGZ"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:2EGZ"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:2EGZ"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:2YSW"
FT HELIX 206..216
FT /evidence="ECO:0007829|PDB:2EGZ"
SQ SEQUENCE 219 AA; 24971 MW; 144C4D5240C86F46 CRC64;
MLIAVPLDDT NFSENLKKAK EKGADIVELR VDQFSDTSLN YVKEKLEEVH SQGLKTILTI
RSPEEGGREV KNREELFEEL SPLSDYTDIE LSSRGLLVKL YNITKEAGKK LIISYHNFEL
TPPNWIIREV LREGYRYGGI PKIAVKANSY EDVARLLCIS RQVEGEKILI SMGDYGKISR
LAGYVFGSVI TYCSLEKAFA PGQIPLEEMV ELRKKFYRL
