3DHQ2_ASPFU
ID 3DHQ2_ASPFU Reviewed; 150 AA.
AC Q4WZ01;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=AFUA_3G14850;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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; AAHF01000002; EAL92102.1; -; Genomic_DNA.
DR RefSeq; XP_754140.1; XM_749047.1.
DR AlphaFoldDB; Q4WZ01; -.
DR SMR; Q4WZ01; -.
DR STRING; 746128.CADAFUBP00003363; -.
DR EnsemblFungi; EAL92102; EAL92102; AFUA_3G14850.
DR GeneID; 3512281; -.
DR KEGG; afm:AFUA_3G14850; -.
DR VEuPathDB; FungiDB:Afu3g14850; -.
DR eggNOG; ENOG502S1A9; Eukaryota.
DR HOGENOM; CLU_090968_1_0_1; -.
DR InParanoid; Q4WZ01; -.
DR OMA; VIECHIS; -.
DR OrthoDB; 1284624at2759; -.
DR UniPathway; UPA00088; UER00178.
DR Proteomes; UP000002530; Chromosome 3.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IBA:GO_Central.
DR GO; GO:0046279; P:3,4-dihydroxybenzoate 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 3: Inferred from homology;
KW Lyase; Quinate metabolism; Reference proteome.
FT CHAIN 1..150
FT /note="Catabolic 3-dehydroquinase 2"
FT /id="PRO_0000402355"
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 150 AA; 16445 MW; 3EE091E734AC90E3 CRC64;
MPSILLINGP NLNLLGTREP HLYGRTTLPQ LEDNAKALAA AKGVKLESFH SNHEGRIIDR
IHEARGHTDA IIINPGAFTH TSVAIRDALI GVSVPFIEVH ITNVHAREEF RHHSYLSDKA
AACIIGLGTY GYEAAIEYAA REIISAKEVY
