AROQ_ACTPL
ID AROQ_ACTPL Reviewed; 154 AA.
AC P43877;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 104.
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;
OS Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=715;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27088 / DSM 13472 / CCM 5869 / S4074 / Serotype 1;
RX PubMed=8170389; DOI=10.1111/j.1365-2958.1994.tb00307.x;
RA Lalonde G., O'Hanley P.D., Stocker B.A.D., Denich K.T.;
RT "Characterization of a 3-dehydroquinase gene from Actinobacillus
RT pleuropneumoniae with homology to the eukaryotic genes qa-2 and QUTE.";
RL Mol. Microbiol. 11:273-280(1994).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND SUBUNIT.
RX PubMed=14993670; DOI=10.1107/s090744490302969x;
RA Maes D., Gonzalez-Ramirez L.A., Lopez-Jaramillo J., Yu B., De Bondt H.,
RA Zegers I., Afonina E., Garcia-Ruiz J.M., Gulnik S.;
RT "Structural study of the type II 3-dehydroquinate dehydratase from
RT Actinobacillus pleuropneumoniae.";
RL Acta Crystallogr. D 60:463-471(2004).
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:0000269|PubMed:14993670}.
CC -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
CC {ECO:0000305}.
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DR EMBL; L19895; AAA72027.1; -; Genomic_DNA.
DR PIR; S41538; S41538.
DR RefSeq; WP_005599518.1; NZ_UIFY01000002.1.
DR PDB; 1UQR; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J/K/L=1-154.
DR PDBsum; 1UQR; -.
DR AlphaFoldDB; P43877; -.
DR SMR; P43877; -.
DR STRING; 228399.appser1_19870; -.
DR GeneID; 66258657; -.
DR OMA; AYTHYSY; -.
DR UniPathway; UPA00053; UER00086.
DR EvolutionaryTrace; P43877; -.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Lyase.
FT CHAIN 1..154
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_0000159862"
FT ACT_SITE 23
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 100
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 101..102
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 18
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1UQR"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:1UQR"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:1UQR"
FT HELIX 28..41
FT /evidence="ECO:0007829|PDB:1UQR"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:1UQR"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:1UQR"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:1UQR"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:1UQR"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:1UQR"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:1UQR"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:1UQR"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:1UQR"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:1UQR"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:1UQR"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:1UQR"
FT HELIX 130..144
FT /evidence="ECO:0007829|PDB:1UQR"
FT HELIX 147..151
FT /evidence="ECO:0007829|PDB:1UQR"
SQ SEQUENCE 154 AA; 17179 MW; 6DDC809E9B276BC4 CRC64;
MKKILLLNGP NLNMLGKREP HIYGSQTLSD IEQHLQQSAQ AQGYELDYFQ ANGEESLINR
IHQAFQNTDF IIINPGAFTH TSVAIRDALL AVSIPFIEVH LSNVHAREPF RHHSYLSDVA
KGVICGLGAK GYDYALDFAI SELQKIQLGE MMNG
