AROQ1_PSEAE
ID AROQ1_PSEAE Reviewed; 147 AA.
AC O30557;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=3-dehydroquinate dehydratase 1;
DE Short=3-dehydroquinase 1;
DE EC=4.2.1.10;
DE AltName: Full=Type II DHQase 1;
GN Name=aroQ1; Synonyms=aroQ; OrderedLocusNames=PA4846;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9353916; DOI=10.1099/00221287-143-10-3111;
RA Page M.D., Saunders N.F.W., Ferguson S.J.;
RT "Disruption of the Pseudomonas aeruginosa dipZ gene, encoding a putative
RT protein-disulfide reductase, leads to partial pleiotropic deficiency in c-
RT type cytochrome biogenesis.";
RL Microbiology 143:3111-3122(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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}.
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DR EMBL; AF010322; AAB84085.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG08231.1; -; Genomic_DNA.
DR PIR; F83039; F83039.
DR RefSeq; NP_253533.1; NC_002516.2.
DR RefSeq; WP_003095385.1; NZ_QZGE01000002.1.
DR PDB; 4L8L; X-ray; 1.74 A; A=3-145.
DR PDBsum; 4L8L; -.
DR AlphaFoldDB; O30557; -.
DR SMR; O30557; -.
DR STRING; 287.DR97_2197; -.
DR PaxDb; O30557; -.
DR PRIDE; O30557; -.
DR DNASU; 878093; -.
DR EnsemblBacteria; AAG08231; AAG08231; PA4846.
DR GeneID; 878093; -.
DR KEGG; pae:PA4846; -.
DR PATRIC; fig|208964.12.peg.5078; -.
DR PseudoCAP; PA4846; -.
DR HOGENOM; CLU_090968_1_0_6; -.
DR InParanoid; O30557; -.
DR OMA; AYTHYSY; -.
DR PhylomeDB; O30557; -.
DR BioCyc; PAER208964:G1FZ6-4960-MON; -.
DR BRENDA; 4.2.1.10; 5087.
DR UniPathway; UPA00053; UER00086.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IBA:GO_Central.
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 GO; GO:0019631; P:quinate catabolic process; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..147
FT /note="3-dehydroquinate dehydratase 1"
FT /id="PRO_0000159918"
FT ACT_SITE 23
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 101
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 102..103
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 112
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:4L8L"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:4L8L"
FT HELIX 28..41
FT /evidence="ECO:0007829|PDB:4L8L"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:4L8L"
FT HELIX 54..66
FT /evidence="ECO:0007829|PDB:4L8L"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:4L8L"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:4L8L"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:4L8L"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:4L8L"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:4L8L"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:4L8L"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:4L8L"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:4L8L"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:4L8L"
SQ SEQUENCE 147 AA; 16234 MW; AA58F827024C85DE CRC64;
MATLLVLHGP NLNLLGTREP GTYGSTTLGQ INQDLERRAR EAGHHLLHLQ SNAEYELIDR
IHAARDEGVD FIIINPAAFT HTSVALRDAL LAVSIPFIEV HLSNVHKREP FRHHSYFSDV
AVGVICGLGA TGYRLALESA LEQLQRP
