3DHQ_SCLS1
ID 3DHQ_SCLS1 Reviewed; 154 AA.
AC A7F996;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=SS1G_14177;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476650; EDO00307.1; -; Genomic_DNA.
DR RefSeq; XP_001584894.1; XM_001584844.1.
DR AlphaFoldDB; A7F996; -.
DR SMR; A7F996; -.
DR STRING; 665079.A7F996; -.
DR GeneID; 5480949; -.
DR KEGG; ssl:SS1G_14177; -.
DR VEuPathDB; FungiDB:sscle_08g068230; -.
DR InParanoid; A7F996; -.
DR OMA; AYTHYSY; -.
DR UniPathway; UPA00088; UER00178.
DR Proteomes; UP000001312; Unassembled WGS sequence.
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..154
FT /note="Catabolic 3-dehydroquinase"
FT /id="PRO_0000402378"
FT ACT_SITE 25
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT ACT_SITE 105
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT BINDING 106..107
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
FT SITE 20
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03136"
SQ SEQUENCE 154 AA; 17142 MW; D8CC05B04DF20989 CRC64;
MPIKKILLLN GPNLNLLGTR EPHIYGYDTL ASIESSLSTY LSSLTPSVEL LTFQSNWEGA
LIDRIHEART DGTDAIVINP AAFTHYSVAL RDALTGVDIP FVEVHISNVH KREEFRHKSF
LSDKAEAVIC GLGVFGYRAA VEWCVGYLKE RPKL
