AROQ_JANSC
ID AROQ_JANSC Reviewed; 148 AA.
AC Q28PZ5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_00169};
DE Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00169};
DE EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_00169};
DE AltName: Full=Type II DHQase {ECO:0000255|HAMAP-Rule:MF_00169};
GN Name=aroQ {ECO:0000255|HAMAP-Rule:MF_00169}; OrderedLocusNames=Jann_2300;
OS Jannaschia sp. (strain CCS1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia; unclassified Jannaschia.
OX NCBI_TaxID=290400;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCS1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W.,
RA Buchan A., Gonzalez J.M., Schell M.A., Richardson P.;
RT "Complete sequence of chromosome of Jannaschia sp. CCS1.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate.
CC {ECO:0000255|HAMAP-Rule:MF_00169}.
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_00169};
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_00169}.
CC -!- SUBUNIT: Homododecamer. {ECO:0000255|HAMAP-Rule:MF_00169}.
CC -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00169}.
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DR EMBL; CP000264; ABD55217.1; -; Genomic_DNA.
DR RefSeq; WP_011455421.1; NC_007802.1.
DR AlphaFoldDB; Q28PZ5; -.
DR SMR; Q28PZ5; -.
DR STRING; 290400.Jann_2300; -.
DR EnsemblBacteria; ABD55217; ABD55217; Jann_2300.
DR KEGG; jan:Jann_2300; -.
DR eggNOG; COG0757; Bacteria.
DR HOGENOM; CLU_090968_1_0_5; -.
DR OMA; CAGIVIN; -.
DR OrthoDB; 1872106at2; -.
DR UniPathway; UPA00053; UER00086.
DR Proteomes; UP000008326; 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; 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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Reference proteome.
FT CHAIN 1..148
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_1000071581"
FT ACT_SITE 22
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT ACT_SITE 99
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 100..101
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT SITE 17
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
SQ SEQUENCE 148 AA; 15553 MW; DCB39523EBBE90F1 CRC64;
MKISVFNGPN LNALGTREPG IYGADTLADI EAACRTTAAD LGVDLDFLQT NQEGALVDAF
HAARDTSDGV VINAGAYTHT SIALRDAISA TELPTVELHL SNTHAREAFR HHSMIAPVCV
GLILGFGAYG YPLAVTALVQ HLKQGNAP
