NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1007/BF00337715; PubMed=2976880 [NCBI, ExPASy, EBI, Israel, Japan]
Hawkins A.R., Lamb H.K., Smith M., Keyte J.W., Roberts C.F.;
"Molecular organisation of the quinic acid utilization (QUT) gene cluster in Aspergillus nidulans.";
Mol. Gen. Genet. 214:224-231(1988).

Comments

CATALYTIC ACTIVITY: Quinate + NAD⁺ = 3-dehydroquinate + NADH.
PATHWAY: Aromatic compound metabolism; 3,4-dihydroxybenzoate biosynthesis; 3-dehydroquinate from quinate (NAD route): step 1/1 .

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X13525; CAA31880.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S08499; S08499.

3D structure databases

HSSP

Q58484; 1NVT. [HSSP ENTRY / PDB]

ModBase

P25415.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0030266;	Molecular function: quinate 5-dehydrogenase activity (inferred from electronic annotation from EC).
GO:0004764;	Molecular function: shikimate 5-dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0019630;	Biological process: quinate metabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR013708; Shikimate_DHase-bd_N.
IPR006151; Shikm_DHase/Glu-tRNA_Rdtase.
Graphical view of domain structure.

Pfam

PF01488; Shikimate_DH; 1.
PF08501; Shikimate_dh_N; 1.
Pfam graphical view of domain structure.

ProtoNet

P25415.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

NAD; Oxidoreductase; Quinate metabolism.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 329`	`329`		`Quinate dehydrogenase.`	`PRO_0000079892`

Sequence information

Length: 329 AA [This is the length of the unprocessed precursor]

Molecular weight: 36031 Da [This is the MW of the unprocessed precursor]

CRC64: 634E50572F1280C5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEPITIPTDR DGVAYLYGHP LPNSLSPPLH QTVYNALGLN WTQIPLSTAT GTSFTRSPEI 

        70         80         90        100        110        120 
STFLSSVRSN PKFVGSSVTM PWKVAIMPHL DDLTEDARQA GACNTIYLRK EDDGKTQYVG 

       130        140        150        160        170        180 
TNTDCIGIRE ALLQGSPNGA EHFKGKPALI VGGGGTARTA IYVLRKWLGV SKIYIVNRDA 

       190        200        210        220        230        240 
KEVEAILAED KQRNPSPQVA LVPVSDPSAA ATLEAPVAVV SGIPNYPPQT EEEIRARETL 

       250        260        270        280        290        300 
RLFLNRQTHE KDQGVILEMC YHPLPWTDIA QIAQDARWKV ILGSEALIWQ GLEQARVWTG 

       310        320 
KDVVSEPGLV EKVQAFVAQT IAERSKSNL

P25415 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools