AROQ_CITK8
ID AROQ_CITK8 Reviewed; 150 AA.
AC A8AQF2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=CKO_04665;
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=290338;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG The Citrobacter koseri Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (AUG-2007) 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; CP000822; ABV15715.1; -; Genomic_DNA.
DR RefSeq; WP_012135390.1; NC_009792.1.
DR AlphaFoldDB; A8AQF2; -.
DR SMR; A8AQF2; -.
DR STRING; 290338.CKO_04665; -.
DR EnsemblBacteria; ABV15715; ABV15715; CKO_04665.
DR GeneID; 45138192; -.
DR KEGG; cko:CKO_04665; -.
DR HOGENOM; CLU_090968_1_0_6; -.
DR OMA; AYTHYSY; -.
DR OrthoDB; 1872106at2; -.
DR BRENDA; 4.2.1.10; 1399.
DR UniPathway; UPA00053; UER00086.
DR Proteomes; UP000008148; 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; 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..150
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_1000023461"
FT ACT_SITE 26
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT ACT_SITE 103
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 104..105
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT SITE 21
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
SQ SEQUENCE 150 AA; 16520 MW; FD4BD2CEF7CDED82 CRC64;
MADKLHILLL NGPNLNMLGT REPDKYGTLT LTEIVNRLNA EADALNVTLD HLQSNAEYAL
IDRIHQAKDT VDYILINPAA FTHTSVAIRD ALLAVSIPFI EIHLSNVHAR EPFRQHSYLS
DIAAGVICGF GADGYSYALQ TAVKRLSQSH
