ID   3DHQ2_ASPTN             Reviewed;         147 AA.
AC   P0CI63; Q0CF61;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Catabolic 3-dehydroquinase 2 {ECO:0000255|HAMAP-Rule:MF_03136};
DE            Short=cDHQase 2 {ECO:0000255|HAMAP-Rule:MF_03136};
DE            EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_03136};
DE   AltName: Full=3-dehydroquinate dehydratase 2 {ECO:0000255|HAMAP-Rule:MF_03136};
GN   Name=qutE2 {ECO:0000255|HAMAP-Rule:MF_03136}; ORFNames=ATEG_07673.2;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAU31935.1; Type=Erroneous gene model prediction; Note=The predicted gene ATEG_07673 has been split into 2 genes: ATEG_07673.1 and ATEG_07673.2.; Evidence={ECO:0000305};
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DR   EMBL; CH476604; EAU31935.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; P0CI63; -.
DR   SMR; P0CI63; -.
DR   EnsemblFungi; EAU31935; EAU31935; ATEG_07673.
DR   OrthoDB; 1537005at2759; -.
DR   UniPathway; UPA00088; UER00178.
DR   Proteomes; UP000007963; 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..147
FT                   /note="Catabolic 3-dehydroquinase 2"
FT                   /id="PRO_0000402438"
FT   ACT_SITE        23
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT   ACT_SITE        100
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT   BINDING         80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT   BINDING         101..102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT   SITE            18
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
SQ   SEQUENCE   147 AA;  16216 MW;  41F3FD81FF8ADB91 CRC64;
     MPSLLLINGP NLNLLGTREP HLYGATTLRD VEEMSRVQAN NYGIDLETFQ SNHEGHIIDR
     IHSARGHIDV IIINPGALTH TSVGLRDALV GVSIPFIEVH ITNVHAREPF RHHSYLSDKA
     SAILVGLGTY GYEAAIQHAA KNMIRKN