AROQ_BUCAP
ID AROQ_BUCAP Reviewed; 149 AA.
AC Q8K9F1;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 107.
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=BUsg_386;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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:0000250}.
CC -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM67938.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE013218; AAM67938.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_044006091.1; NC_004061.1.
DR AlphaFoldDB; Q8K9F1; -.
DR SMR; Q8K9F1; -.
DR STRING; 198804.BUsg_386; -.
DR EnsemblBacteria; AAM67938; AAM67938; BUsg_386.
DR KEGG; bas:BUsg_386; -.
DR eggNOG; COG0757; Bacteria.
DR HOGENOM; CLU_090968_3_0_6; -.
DR OMA; AYTHYSY; -.
DR OrthoDB; 1872106at2; -.
DR UniPathway; UPA00053; UER00086.
DR Proteomes; UP000000416; 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 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase.
FT CHAIN 1..149
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_0000159884"
FT ACT_SITE 26
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 104
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 105..106
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 21
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 149 AA; 16788 MW; 350A531FF97F6594 CRC64;
MKKNINVLLI NGPNLNLLGD REKNIYGDKT LSCLINDLKK RSEILNISLN DIQSNAEHVI
IEKIHSAKKE KIDYIIINPA AFTHTSIAIR DALIAVTIPF IEVHISNIYA RENFRSHSWL
SDISKGVITG LGLDGYFWAL ETISKRCCV
