AROD_LACLA
ID AROD_LACLA Reviewed; 226 AA.
AC Q9CF39;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=LL1642;
GN ORFNames=L0062;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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; AE005176; AAK05740.1; -; Genomic_DNA.
DR PIR; B86830; B86830.
DR RefSeq; NP_267798.1; NC_002662.1.
DR RefSeq; WP_003129440.1; NC_002662.1.
DR AlphaFoldDB; Q9CF39; -.
DR SMR; Q9CF39; -.
DR STRING; 272623.L0062; -.
DR PaxDb; Q9CF39; -.
DR EnsemblBacteria; AAK05740; AAK05740; L0062.
DR GeneID; 60355535; -.
DR KEGG; lla:L0062; -.
DR PATRIC; fig|272623.7.peg.1764; -.
DR eggNOG; COG0710; Bacteria.
DR HOGENOM; CLU_064444_0_0_9; -.
DR OMA; FATMSMG; -.
DR UniPathway; UPA00053; UER00086.
DR Proteomes; UP000002196; 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..226
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_0000138797"
FT ACT_SITE 121
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT ACT_SITE 146
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 33..35
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 65
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 188
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 207
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
FT BINDING 211
FT /ligand="3-dehydroquinate"
FT /ligand_id="ChEBI:CHEBI:32364"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00214"
SQ SEQUENCE 226 AA; 25974 MW; F6D97B3098E7F5F1 CRC64;
MRKTKIVVPI MLTELAELEK VSVSDYRTAD IVEWRADFLS ADEILEMAPK FFEKFKESKI
LFTLRTVREG GNIQVSEKKY LQILKEILTY NPAYIDVEFF THGPSFAALK DFRDKMVLSY
HNFDEVPSDL TNRLIKMHEE GTAFVKVAVM PERECDVLDL LQITRDMTLE YGDHFISMAM
GDLGRLSRIS GYLTGSCWTF ASLENSSAPG QISLKETEYI LDILEK
