Reviewed, UniProtKB/Swiss-Prot P05147 (3DHQ_EMENI)

Names and origin

Protein names

Recommended name:
    Catabolic 3-dehydroquinase
    EC=4.2.1.10
Alternative name(s):
    3-dehydroquinate dehydratase

Gene names

Name:	qutE
ORF Names:	AN1135

Organism

Emericella nidulans (Aspergillus nidulans) [Complete proteome]

Taxonomic identifier

162425 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	153 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Is involved in the catabolism of quinate.
Catalytic activity	3-dehydroquinate = 3-dehydroshikimate + H2O.
Pathway	Aromatic compound metabolism; 3,4-dihydroxybenzoate biosynthesis; 3,4-dihydroxybenzoate from 3-dehydroquinate: step 1/2.
Subunit structure	Homododecamer Probable.
Sequence similarities	Belongs to the type-II 3-dehydroquinase family.

Ontologies

Keywords
Biological process	Quinate metabolism
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	quinate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	3-dehydroquinate dehydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 153	153	Catabolic 3-dehydroquinase		PRO_0000159947
Regions
	Region	102 – 103	2	Substrate binding By similarity
Sites
	Active site	24	1	Proton acceptor By similarity
	Active site	101	1	Proton donor By similarity
	Binding site	75	1	Substrate By similarity
	Binding site	81	1	Substrate By similarity
	Binding site	88	1	Substrate By similarity
	Binding site	112	1	Substrate By similarity
	Site	19	1	Transition state stabilizer By similarity
Experimental info
	Sequence conflict	60	1	D → E in CAA31881. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P05147-1 [UniParc]. Last modified May 1, 2007. Version 3. Checksum: 86B661A3D1788F47	FASTA	153	16,503
	10 20 30 40 50 60 MEKSILLING PNLNLLGTRE PHIYGSTTLS DVEESSKGHA ASLGASLQTF QSNHEGAIVD 70 80 90 100 110 120 RIHAARGNTD AIIINPGAYT HTSVAIRDAL LGVEIPFIEL HVSNVHAREP FRHHSYFSDK 130 140 150 ASGIIVGLGV YGYKVAVEHV ALNFKPLEKK AAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular organisation of the quinic acid utilization (QUT) gene cluster in Aspergillus nidulans." Hawkins A.R., Lamb H.K., Smith M., Keyte J.W., Roberts C.F. Mol. Gen. Genet. 214:224-231(1988) [PubMed: 2976880] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequence analysis and transformation by the catabolic 3-dehydroquinase (QUTE) gene from Aspergillus nidulans." da Silva A.J.F., Whittington H., Clements J., Roberts C.F., Hawkins A.R. Biochem. J. 240:481-488(1986) [PubMed: 2949740] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: R153.
[3]	Hawkins A.R. Submitted (APR-1987) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[4]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC 4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X13525 Genomic DNA. Translation: CAA31881.1. X04696 Genomic DNA. Translation: CAA28401.1. AACD01000016 Genomic DNA. Translation: EAA66253.1.
PIR	S08501.
RefSeq	XP_658739.1.
3D structure databases
HSSP	HSSP built from PDB template 1GU1 based on UniProtKB P15474.
ModBase	Search...
Genome annotation databases
GeneID	2876911.
KEGG	ani:AN1135.2.
Enzyme and pathway databases
BRENDA	4.2.1.10. 3859.
Family and domain databases
InterPro	IPR001874. DHquinase_II. IPR018509. DHquinase_II_CS. [Graphical view]
Gene3D	G3DSA:3.40.50.9100. DHquinase_II. 1 hit.
PANTHER	PTHR21272. DHquinase_II. 1 hit.
Pfam	PF01220. DHquinase_II. 1 hit. [Graphical view]
PIRSF	PIRSF001399. DHquinase_II. 1 hit.
ProDom	PD004527. DHquinase_II. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01088. aroQ. 1 hit.
PROSITE	PS01029. DEHYDROQUINASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

3DHQ_EMENI

Accession

Primary (citable) accession number: P05147
Secondary accession number(s): Q5BE95

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	May 1, 2007
Last modified:	September 22, 2009
This is version 63 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)