AROD_DEHM1
ID AROD_DEHM1 Reviewed; 222 AA.
AC Q3Z989;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=DET0466;
OS Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195)
OS (Dehalococcoides ethenogenes (strain 195)).
OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalococcoides.
OX NCBI_TaxID=243164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2266 / KCTC 15142 / 195;
RX PubMed=15637277; DOI=10.1126/science.1102226;
RA Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A.,
RA Ward N.L., Nelson W.C., DeBoy R.T., Khouri H.M., Kolonay J.F., Dodson R.J.,
RA Daugherty S.C., Brinkac L.M., Sullivan S.A., Madupu R., Nelson K.E.,
RA Kang K.H., Impraim M., Tran K., Robinson J.M., Forberger H.A., Fraser C.M.,
RA Zinder S.H., Heidelberg J.F.;
RT "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT ethenogenes.";
RL Science 307:105-108(2005).
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 -!- SIMILARITY: Belongs to the type-I 3-dehydroquinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00214}.
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DR EMBL; CP000027; AAW40205.1; -; Genomic_DNA.
DR RefSeq; WP_010936243.1; NC_002936.3.
DR AlphaFoldDB; Q3Z989; -.
DR SMR; Q3Z989; -.
DR STRING; 243164.DET0466; -.
DR EnsemblBacteria; AAW40205; AAW40205; DET0466.
DR KEGG; det:DET0466; -.
DR PATRIC; fig|243164.10.peg.444; -.
DR eggNOG; COG0710; Bacteria.
DR HOGENOM; CLU_064444_2_1_0; -.
DR OMA; ATMAMGE; -.
DR OrthoDB; 1298468at2; -.
DR UniPathway; UPA00053; UER00086.
DR Proteomes; UP000008289; Chromosome.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046279; P:3,4-dihydroxybenzoate biosynthetic process; IEA:UniProt.
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; IPR013785; Aldolase_TIM.
DR InterPro; IPR001381; DHquinase_I.
DR Pfam; PF01487; DHquinase_I; 1.
DR TIGRFAMs; TIGR01093; aroD; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Reference proteome; Schiff base.
FT CHAIN 1..222
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_0000325522"
FT ACT_SITE 112
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT ACT_SITE 139
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 29..31
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 55
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 178
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 199
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 203
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
SQ SEQUENCE 222 AA; 24366 MW; B174BD2BA2BC2266 CRC64;
MKNPPVCCVI TRLPEAESLK KSEGAAFYEL RLDLLGESWR EAAAMLDKPF MATCRRSAEG
GSFSGSEEER IGLLEKAAAA GAFMLDIEYS TPHLGEVLKR LRTQSKCLVS HHNFADTPSA
GDLKTLVKDM LNYPADIYKV ITTATSINDN IKLLNLIKEI PDKKIVAFAM GNLGILSRIL
CPLAGSPFTY ASLNDSNQSA SGQMTLAQMI EIYRSVNYEN HT
