3DHQ1_FUSV7
ID 3DHQ1_FUSV7 Reviewed; 144 AA.
AC C7ZKL6;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 52.
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}; ORFNames=NECHADRAFT_51144;
OS Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL
OS 45880 / 77-13-4) (Fusarium solani subsp. pisi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex; Fusarium vanettenii.
OX NCBI_TaxID=660122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4;
RX PubMed=19714214; DOI=10.1371/journal.pgen.1000618;
RA Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A., Wasmann C.C.,
RA Grimwood J., Schmutz J., Taga M., White G.J., Zhou S., Schwartz D.C.,
RA Freitag M., Ma L.-J., Danchin E.G.J., Henrissat B., Coutinho P.M.,
RA Nelson D.R., Straney D., Napoli C.A., Barker B.M., Gribskov M., Rep M.,
RA Kroken S., Molnar I., Rensing C., Kennell J.C., Zamora J., Farman M.L.,
RA Selker E.U., Salamov A., Shapiro H., Pangilinan J., Lindquist E.,
RA Lamers C., Grigoriev I.V., Geiser D.M., Covert S.F., Temporini E.,
RA VanEtten H.D.;
RT "The genome of Nectria haematococca: contribution of supernumerary
RT chromosomes to gene expansion.";
RL PLoS Genet. 5:E1000618-E1000618(2009).
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; GG698940; EEU35430.1; -; Genomic_DNA.
DR RefSeq; XP_003041143.1; XM_003041097.1.
DR AlphaFoldDB; C7ZKL6; -.
DR SMR; C7ZKL6; -.
DR STRING; 140110.NechaP51144; -.
DR EnsemblFungi; NechaT51144; NechaP51144; NechaG51144.
DR GeneID; 9675703; -.
DR KEGG; nhe:NECHADRAFT_51144; -.
DR eggNOG; ENOG502S1A9; Eukaryota.
DR HOGENOM; CLU_090968_1_0_1; -.
DR InParanoid; C7ZKL6; -.
DR OMA; CAGIVIN; -.
DR OrthoDB; 1284624at2759; -.
DR UniPathway; UPA00088; UER00178.
DR Proteomes; UP000005206; 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..144
FT /note="Catabolic 3-dehydroquinase 1"
FT /id="PRO_0000402367"
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 144 AA; 15889 MW; 601EBD9EE6C062D2 CRC64;
MGHSVLLING PNLNLLGTRE PHIYGHTTLK DLEESCKEHA QSLGAELQSF QSNAEGTIID
RIHEARGKID VIIINPAGYT HTSVAIRDAL AGVDIPFIEL HISNTHTREK FRHHSYLSDK
AAAVIMGFGV DGYKYAVDYA VRNL
