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Reviewed, UniProtKB/Swiss-Prot P05195 (3DHQ_NEUCR)

Last modified September 1, 2009. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Catabolic 3-dehydroquinase
    EC=4.2.1.10
Alternative name(s):
    3-dehydroquinate dehydratase
Gene names
Name: qa-2
ORF Names: NCU06023
OrganismNeurospora crassa [Complete proteome]
Taxonomic identifier5141 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora

Protein attributes

Sequence length173 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred 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 processQuinate metabolism
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processquinate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function3-dehydroquinate dehydratase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 173173Catabolic 3-dehydroquinase
PRO_0000159948

Regions

Region129 – 1302Substrate binding By similarity

Sites

Active site261Proton acceptor By similarity
Active site1281Proton donor By similarity
Binding site1021Substrate By similarity
Binding site1081Substrate By similarity
Binding site1151Substrate By similarity
Binding site1391Substrate By similarity
Site211Transition state stabilizer By similarity

Experimental info

Sequence conflict25 – 295IYGST → STAQS in CAA24237. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P05195-1 [UniParc].

Last modified October 1, 1989. Version 2.
Checksum: 6A6EC7594DD46F1B

FASTA17318,272
        10         20         30         40         50         60 
MASPRHILLI NGPNLNLLGT REPQIYGSTT LHDIEQASQT LASSLGLRLT TFQSNHEGAI 

        70         80         90        100        110        120 
IDRIHQAAGF VPSPPSPSPS SAATTTEAGL GPGDKVSAII INPGAYTHTS IGIRDALLGT 

       130        140        150        160        170 
GIPFVEVHVS NVHAREAFRH HSYLSDKAVA VICGLGPFGY SAALDFLGRH MKF 

« Hide

References

« Hide 'large scale' references
[1]"DNA sequence, organization and regulation of the qa gene cluster of Neurospora crassa."
Geever R.F., Huiet L., Baum J.A., Tyler B.M., Patel V.B., Rutledge B.J., Case M.E., Giles N.H.
J. Mol. Biol. 207:15-34(1989) [PubMed: 2525625] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[2]"The genome sequence of the filamentous fungus Neurospora crassa."
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. expand/collapse author list , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
Nature 422:859-868(2003) [PubMed: 12712197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[3]"5'-Untranslated sequences of two structural genes in the qa gene cluster of Neurospora crassa."
Alton N.K., Buxton F., Patel V., Giles N.H., Vapnek D.
Proc. Natl. Acad. Sci. U.S.A. 79:1955-1959(1982) [PubMed: 6210913] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-124.

Cross-references

Sequence databases

X14603 Genomic DNA. Translation: CAA32749.1.
V00869 Genomic DNA. Translation: CAA24237.1.
AABX02000021 Genomic DNA. Translation: EAA30377.1.
PIRA31277. S04251.
RefSeqXP_959613.1.

3D structure databases

HSSPHSSP built from PDB template 1GU1 based on UniProtKB P15474.
ModBaseSearch...

Protein-protein interaction databases

STRINGP05195.

Genome annotation databases

GeneID3875772.
KEGGncr:NCU06023.
NMPDRfig|5141.1.peg.3811.

Enzyme and pathway databases

BioCycNCRA-XX3-01:NCRA-XX3-01-009771-MON.
BRENDA4.2.1.10. 266.

Family and domain databases

InterProIPR001874. DHquinase_II.
IPR018509. DHquinase_II_CS.
[Graphical view]
PANTHERPTHR21272. DHquinase_II. 1 hit.
PfamPF01220. DHquinase_II. 1 hit.
[Graphical view]
PIRSFPIRSF001399. DHquinase_II. 1 hit.
ProDomPD004527. DHquinase_II. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01088. aroQ. 1 hit.
PROSITEPS01029. DEHYDROQUINASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry name3DHQ_NEUCR
AccessionPrimary (citable) accession number: P05195
Secondary accession number(s): Q7RVA3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: October 1, 1989
Last modified: September 1, 2009
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents