ID 3DHQ_EMENI STANDARD; PRT; 153 AA. AC P05147; DT 13-AUG-1987 (Rel. 05, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 25-OCT-2004 (Rel. 45, Last annotation update) DE Catabolic 3-dehydroquinase (EC 4.2.1.10) (3-dehydroquinate DE dehydratase). GN Name=qutE; OS Emericella nidulans (Aspergillus nidulans). OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; Emericella. OX NCBI_TaxID=162425; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=89181521; PubMed=2976880; RA Hawkins A.R., Lamb H.K., Smith M., Keyte J.W., Roberts C.F.; RT "Molecular organisation of the quinic acid utilization (QUT) gene RT cluster in Aspergillus nidulans."; RL Mol. Gen. Genet. 214:224-231(1988). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=R153; RX MEDLINE=87127965; PubMed=2949740; RA da Silva A.J.F., Whittington H., Clements J., Roberts C.F., RA Hawkins A.R.; RT "Sequence analysis and transformation by the catabolic 3- RT dehydroquinase (QUTE) gene from Aspergillus nidulans."; RL Biochem. J. 240:481-488(1986). RN [3] RP SEQUENCE REVISION. RA Hawkins A.R.; RL Submitted (APR-1987) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Is involved in the catabolism of quinate. CC -!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O. CC -!- PATHWAY: Quinic acid catabolic pathway; second step. This pathway CC allows use of quinate as a carbon source by its conversion to CC protocatechuate and subsequent metabolism by the beta-ketoadipate CC pathway. CC -!- SUBUNIT: Homododecamer (Probable). CC -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13525; CAA31881.1; -. DR EMBL; X04696; CAA28401.1; -. DR PIR; S08501; S08501. DR HSSP; P15474; 1GU1. DR InterPro; IPR001874; DHquinase_II. DR Pfam; PF01220; DHquinase_II; 1. DR ProDom; PD004527; DHquinase_II; 1. DR TIGRFAMs; TIGR01088; aroQ; 1. DR PROSITE; PS01029; DEHYDROQUINASE_II; 1. KW Lyase; Quinate metabolism. FT ACT_SITE 24 24 Nucleophile (By similarity). FT CONFLICT 60 60 E -> D (in Ref. 2). SQ SEQUENCE 153 AA; 16517 MW; 9DACD00961799E46 CRC64; MEKSILLING PNLNLLGTRE PHIYGSTTLS DVEESSKGHA ASLGASLQTF QSNHEGAIVE RIHAARGNTD AIIINPGAYT HTSVAIRDAL LGVEIPFIEL HVSNVHAREP FRHHSYFSDK ASGIIVGLGV YGYKVAVEHV ALNFKPLEKK AAL //