3DHQ_ASPCL
ID 3DHQ_ASPCL Reviewed; 150 AA.
AC A1CPW7;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Catabolic 3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_03136};
DE Short=cDHQase {ECO:0000255|HAMAP-Rule:MF_03136};
DE EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_03136};
DE AltName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_03136};
GN Name=qutE {ECO:0000255|HAMAP-Rule:MF_03136}; ORFNames=ACLA_024030;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- FUNCTION: Is involved in the catabolism of quinate. Allows the
CC utilization of quinate as carbon source via the beta-ketoadipate
CC pathway. {ECO:0000255|HAMAP-Rule:MF_03136}.
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_03136};
CC -!- PATHWAY: Aromatic compound metabolism; 3,4-dihydroxybenzoate
CC biosynthesis; 3,4-dihydroxybenzoate from 3-dehydroquinate: step 1/2.
CC {ECO:0000255|HAMAP-Rule:MF_03136}.
CC -!- SUBUNIT: Homododecamer. Adopts a ring-like structure, composed of an
CC arrangement of two hexameric rings stacked on top of one another.
CC {ECO:0000255|HAMAP-Rule:MF_03136}.
CC -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
CC {ECO:0000255|HAMAP-Rule:MF_03136}.
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DR EMBL; DS027059; EAW07688.1; -; Genomic_DNA.
DR RefSeq; XP_001269114.1; XM_001269113.1.
DR AlphaFoldDB; A1CPW7; -.
DR SMR; A1CPW7; -.
DR STRING; 5057.CADACLAP00003055; -.
DR EnsemblFungi; EAW07688; EAW07688; ACLA_024030.
DR GeneID; 4701115; -.
DR KEGG; act:ACLA_024030; -.
DR VEuPathDB; FungiDB:ACLA_024030; -.
DR eggNOG; ENOG502S1A9; Eukaryota.
DR HOGENOM; CLU_090968_1_0_1; -.
DR OMA; CAGIVIN; -.
DR OrthoDB; 1284624at2759; -.
DR UniPathway; UPA00088; UER00178.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046279; P:3,4-dihydroxybenzoate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019630; P:quinate metabolic process; IEA:UniProtKB-UniRule.
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 Lyase; Quinate metabolism; Reference proteome.
FT CHAIN 1..150
FT /note="Catabolic 3-dehydroquinase"
FT /id="PRO_0000402351"
FT ACT_SITE 24
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT ACT_SITE 101
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT BINDING 102..103
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT SITE 19
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
SQ SEQUENCE 150 AA; 16126 MW; D17F8BD482146150 CRC64;
MGKSILLING PNLNLLGTRE PHIYGSTTLP DIVASSKAHA ESLGATLEAF QSNHEGAIVD
RIQEARGNVD GIVINPGAFT HTSVAIRDAL LAVNIPFIEL HVSNVHAREP WRHHSYFSDK
AAGIIVGLGA YGYKVAVEHV ALNFKERASL
