AROQ_CERS4
ID AROQ_CERS4 Reviewed; 147 AA.
AC Q3IWV4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=RHOS4_34120;
GN ORFNames=RSP_3376;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 2 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000144; ABA80980.1; -; Genomic_DNA.
DR RefSeq; WP_011339256.1; NZ_CP030272.1.
DR RefSeq; YP_354881.1; NC_007494.2.
DR AlphaFoldDB; Q3IWV4; -.
DR SMR; Q3IWV4; -.
DR STRING; 272943.RSP_3376; -.
DR EnsemblBacteria; ABA80980; ABA80980; RSP_3376.
DR KEGG; rsp:RSP_3376; -.
DR PATRIC; fig|272943.9.peg.3813; -.
DR eggNOG; COG0757; Bacteria.
DR OMA; VIECHIS; -.
DR PhylomeDB; Q3IWV4; -.
DR UniPathway; UPA00053; UER00086.
DR Proteomes; UP000002703; Chromosome 2.
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;
KW Reference proteome.
FT CHAIN 1..147
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_1000023507"
FT ACT_SITE 24
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT ACT_SITE 101
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 102..103
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT SITE 19
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
SQ SEQUENCE 147 AA; 15971 MW; 93D0D7A8384232A6 CRC64;
MTTTIYILNG PNLNLLGQRQ PEIYGHETLA DVERRCAAVA AEKGFSVRLF QSNHEGAIVD
QIHEARQAAC GIVINPAAYT HTSVAILDAL NAFEGPVIEC HISNVHKRES FRHHSYVSLR
ADGVLAGFGI EGYELAVRRI CSLCAGG
