3DHQ1_ASPFU
ID 3DHQ1_ASPFU Reviewed; 150 AA.
AC Q6MYX3; Q4WSU3;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Catabolic 3-dehydroquinase 1 {ECO:0000255|HAMAP-Rule:MF_03136};
DE Short=cDHQase 1 {ECO:0000255|HAMAP-Rule:MF_03136};
DE EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_03136};
DE AltName: Full=3-dehydroquinate dehydratase 1 {ECO:0000255|HAMAP-Rule:MF_03136};
GN Name=qutE1 {ECO:0000255|HAMAP-Rule:MF_03136};
GN ORFNames=AfA5A2.045, AFUA_1G11610;
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=14998527; DOI=10.1016/j.fgb.2003.12.003;
RA Pain A., Woodward J.R., Quail M.A., Anderson M.J., Clark R., Collins M.,
RA Fosker N., Fraser A., Harris D.E., Larke N., Murphy L.D., Humphray S.,
RA O'Neil S., Pertea M., Price C., Rabbinowitsch E., Rajandream M.A.,
RA Salzberg S.L., Saunders D., Seeger K., Sharp S., Warren T., Denning D.W.,
RA Barrell B.G., Hall N.;
RT "Insight into the genome of Aspergillus fumigatus: analysis of a 922 kb
RT region encompassing the nitrate assimilation gene cluster.";
RL Fungal Genet. Biol. 41:443-453(2004).
RN [2]
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; BX649605; CAE47886.1; -; Genomic_DNA.
DR EMBL; AAHF01000004; EAL90489.1; -; Genomic_DNA.
DR RefSeq; XP_752527.1; XM_747434.1.
DR AlphaFoldDB; Q6MYX3; -.
DR SMR; Q6MYX3; -.
DR STRING; 746128.CADAFUBP00001085; -.
DR EnsemblFungi; EAL90489; EAL90489; AFUA_1G11610.
DR GeneID; 3510176; -.
DR KEGG; afm:AFUA_1G11610; -.
DR VEuPathDB; FungiDB:Afu1g11610; -.
DR eggNOG; ENOG502S1A9; Eukaryota.
DR HOGENOM; CLU_090968_1_0_1; -.
DR InParanoid; Q6MYX3; -.
DR OMA; CAGIVIN; -.
DR OrthoDB; 1284624at2759; -.
DR UniPathway; UPA00088; UER00178.
DR Proteomes; UP000002530; Chromosome 1.
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 1"
FT /id="PRO_0000402354"
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; 16042 MW; 9C0A9DC3A17A5D8B CRC64;
MGKSILLING PNLNLLGTRE PHIYGNTTLA DVEASCKAHA ESLGATLATF QSNHEGAIID
RIQAARGNVD GIIINPGAFT HTSVAIRDAL LGVGIPFIEL HVSNVHAREP WRHHSYFSDK
AAGIIVGLGV YGYKVAVEHV ALNFKERAAL
