P11635 (DHQA_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Quinate dehydrogenase
EC=1.1.1.24

Gene names

Name:	qa-3
ORF Names:	NCU06025

Organism

Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]

Taxonomic identifier

367110 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora › Neurospora crassa

Protein attributes

Sequence length	339 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	Quinate + NAD+ = 3-dehydroquinate + NADH.
Pathway	Aromatic compound metabolism; 3,4-dihydroxybenzoate biosynthesis; 3-dehydroquinate from D-quinate (NAD(+) route): step 1/1.
Induction	By quinic acid and the positive regulator qa-1f.
Miscellaneous	N.crassa can utilize quinic acid as sole carbon source, oxidizing it to protocatechuic acid and ultimately to succinic acid and acetic acid. The conversion of quinic acid to protocatechuic acid is catalyzed by enzymes which are encoded by three coordinately regulated genes comprising the qa gene cluster.
Caution	It is uncertain whether Met-1 or Met-14 is the initiator.
Sequence caution	The sequence CAA32751.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence EAA30379.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Quinate metabolism
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	quinate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	nucleotide binding Inferred from electronic annotation. Source: InterPro quinate 3-dehydrogenase (NAD+) activity Inferred from electronic annotation. Source: EC shikimate 3-dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 339	339	Quinate dehydrogenase		PRO_0000079893

Sequences

	Sequence		Length	Mass (Da)
	P11635 [UniParc]. Last modified December 4, 2007. Version 2. Checksum: 8A951802A06C03D4	FASTA	339	37,271
	10 20 30 40 50 60 MSTATTTTSA TTTMSVVQPR QQELLHLTST PDITPYTRHG YLFGQKLAAS MSPLLHSIVY 70 80 90 100 110 120 SHLSLNWAQL RLDSPSIPLF LQLAQHPDFY GASVTMPHKV AIIPHLDHLT PECRDVGACN 130 140 150 160 170 180 TLFLKTDPAT GRRLYCGANT DVIGVRESFV QNVSDPARVY ESRPALVIGG GGAARSAVYA 190 200 210 220 230 240 LHKWLGATDI YLVNRDKSEV DAVIAECTER GYGDRLVHVA SVEQAEGLEG PGAIVACIPD 250 260 270 280 290 300 FPPKTEKEML VRRIVETFLM KEEKGAMLEM CYNPSPFTEL GALAEHEGWQ VILGTEALIW 310 320 330 QGIEQDKYWT GRTNEELPIQ QIKEVIAAKL AEASKSHTS

References

	« Hide 'large scale' referencesShow '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] [Europe PMC] [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. , 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X14603 Genomic DNA. Translation: CAA32751.1. Sequence problems. AABX02000021 Genomic DNA. Translation: EAA30379.2. Different initiation.
PIR	S04253.
RefSeq	XP_959615.2. XM_954522.2.
UniGene	Ncr.25298.
3D structure databases
ProteinModelPortal	P11635.
ModBase	Search...
Protein-protein interaction databases
STRING	5141.NCU06025.1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	EFNCRT00000005369; EFNCRP00000005363; EFNCRG00000005362.
GeneID	3875774.
KEGG	ncr:NCU06025.
Phylogenomic databases
eggNOG	COG0169.
HOGENOM	HOG000237875.
KO	K09484.
OrthoDB	EOG4DRDN5.
Enzyme and pathway databases
UniPathway	UPA00088; UER00176.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR016040. NAD(P)-bd_dom. IPR013708. Shikimate_DH-bd_N. IPR006151. Shikm_DH/Glu-tRNA_Rdtase. [Graphical view]
Pfam	PF01488. Shikimate_DH. 1 hit. PF08501. Shikimate_dh_N. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHQA_NEUCR

Accession

Primary (citable) accession number: P11635
Secondary accession number(s): Q7RVA1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	December 4, 2007
Last modified:	April 3, 2013
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program