Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9SQT8 (DHQSD_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase, chloroplastic
Short name=DHQ-SDH protein
Alternative name(s):
DHQase-SORase
Protein EMBRYO DEFECTIVE 3004

Including the following 2 domains:

  1. Dehydroquinate dehydratase
    Short name=DHQ
    EC=4.2.1.10
  2. Shikimate dehydrogenase
    Short name=SDH
    EC=1.1.1.25
Gene names
Name:EMB3004
Ordered Locus Names:At3g06350
ORF Names:F24P17.18
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length603 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

3-dehydroquinate = 3-dehydroshikimate + H2O.

Shikimate + NADP+ = 3-dehydroshikimate + NADPH.

Pathway

Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.

Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.

Subunit structure

Monomer.

Subcellular location

Plastid › chloroplast Potential.

Sequence similarities

In the N-terminal section; belongs to the type-I 3-dehydroquinase family.

In the C-terminal section; belongs to the shikimate dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

KM=685 µM for shikimate Ref.6

KM=131 µM for NADP

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6666Chloroplast Potential
Chain67 – 603537Bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase, chloroplastic
PRO_0000250645

Regions

Region96 – 3132183-dehydroquinate dehydratase
Region328 – 558231Shikimate dehydrogenase

Sites

Active site2141Proton acceptor; for 3-dehydroquinate dehydratase activity
Active site2411Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activity
Active site3851For shikimate dehydrogenase activity
Active site4231For shikimate dehydrogenase activity
Binding site2791Substrate; for 3-dehydroquinate dehydratase activity
Binding site3361Substrate; for shikimate dehydrogenase activity
Binding site3381Substrate; for shikimate dehydrogenase activity
Binding site4061Substrate; for shikimate dehydrogenase activity
Binding site5501Substrate; for shikimate dehydrogenase activity
Binding site5781Substrate; for shikimate dehydrogenase activity
Binding site5821Substrate; for shikimate dehydrogenase activity

Experimental info

Mutagenesis3361S → A: 13-fold decrease in substrate affinity but almost no change in activity. Ref.6
Mutagenesis3381S → A: 10-fold decrease in activity, and 9-fold decrease in substrate affinity. Ref.6
Mutagenesis3851K → A: Strongly reduced shikimate dehydrogenase activity, but minor change in substrate affinity. Ref.6
Mutagenesis3851K → N: Strongly reduced shikimate dehydrogenase activity, but no change in substrate affinity. Ref.6
Mutagenesis4231D → A: Loss of shikimate dehydrogenase activity. Ref.6
Mutagenesis4231D → N: Reduced shikimate dehydrogenase activity, but no change in substrate affinity. Ref.6
Mutagenesis5501Y → F or A: 100-fold decrease in activity, and 2-fold decrease in substrate affinity. Ref.6
Sequence conflict4911E → K in BAD94599. Ref.5
Sequence conflict5571L → Q in AAS76684. Ref.3

Secondary structure

1 ................................................................................................ 603
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9SQT8 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 4DAAB35F594E7CB6

FASTA60365,796
        10         20         30         40         50         60 
MAASSTNARL TNPPRLLSKP RLSPTSVANL RFPAADFSTR FFADSSSPRL RSVPFPVVFS 

        70         80         90        100        110        120 
DQRRRRSMEP SNVYVASNST EMEIGSHDIV KNPSLICAPV MADSIDKMVI ETSKAHELGA 

       130        140        150        160        170        180 
DLVEIRLDWL KDFNPLEDLK TIIKKSPLPT LFTYRPKWEG GQYEGDENER RDVLRLAMEL 

       190        200        210        220        230        240 
GADYIDVELQ VASEFIKSID GKKPGKFKVI VSSHNYQNTP SVEDLDGLVA RIQQTGADIV 

       250        260        270        280        290        300 
KIATTAVDIA DVARMFHITS KAQVPTIGLV MGERGLMSRI LCSKFGGYLT FGTLDSSKVS 

       310        320        330        340        350        360 
APGQPTIKDL LDLYNFRRIG PDTKVYGIIG KPVSHSKSPI VHNQAFKSVD FNGVYVHLLV 

       370        380        390        400        410        420 
DNLVSFLQAY SSSDFAGFSC TIPHKEAALQ CCDEVDPLAK SIGAVNTILR RKSDGKLLGY 

       430        440        450        460        470        480 
NTDCIGSISA IEDGLRSSGD PSSVPSSSSP LASKTVVVIG AGGAGKALAY GAKEKGAKVV 

       490        500        510        520        530        540 
IANRTYERAL ELAEAIGGKA LSLTDLDNYH PEDGMVLANT TSMGMQPNVE ETPISKDALK 

       550        560        570        580        590        600 
HYALVFDAVY TPRITRLLRE AEESGAITVS GSEMFVRQAY EQFEIFTGLP APKELYWQIM 


SKY

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y., Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M., Shinozaki K., Ecker J.R.
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Shikimate dehydrogenase: a bi-functional enzyme with a novel role in plant and microbial secondary metabolism."
Muir R.M., Ingham E., Uratsu S.L., Leslie C.A., McGranahan G.H., Dandekar A.M.
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 94-603.
[5]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 465-603.
Strain: cv. Columbia.
[6]"Structure of Arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase and implications for metabolic channeling in the shikimate pathway."
Singh S.A., Christendat D.
Biochemistry 45:7787-7796(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 90-603 IN COMPLEX WITH SHIKIMATE AND TARTRATE, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-336; SER-338; LYS-385; ASP-423 AND TYR-550.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AC011623 Genomic DNA. Translation: AAF08579.1.
CP002686 Genomic DNA. Translation: AEE74381.1.
BT012197 mRNA. Translation: AAS76684.1.
AY736474 mRNA. Translation: AAW63134.1.
AK220988 mRNA. Translation: BAD94599.1.
IPIIPI00541842.
RefSeqNP_187286.1. NM_111510.3.
UniGeneAt.43031.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GPTX-ray1.95A90-603[»]
2O7QX-ray2.20A90-603[»]
2O7SX-ray1.78A90-603[»]
ProteinModelPortalQ9SQT8.
SMRQ9SQT8. Positions 90-603.
ModBaseSearch...

Proteomic databases

PaxDbQ9SQT8.
PRIDEQ9SQT8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G06350.1; AT3G06350.1; AT3G06350.
GeneID819809.
KEGGath:AT3G06350.

Organism-specific databases

TAIRAt3g06350.

Phylogenomic databases

eggNOGCOG0169.
HOGENOMHOG000237875.
InParanoidQ9SQT8.
KOK13832.
OMAISHLSHN.
PhylomeDBQ9SQT8.
ProtClustDBPLN02520.

Enzyme and pathway databases

BioCycARA:AT3G06350-MONOMER.
MetaCyc:AT3G06350-MONOMER.
BRENDA4.2.1.10. 399.
UniPathwayUPA00053; UER00086.
UPA00053; UER00087.

Gene expression databases

GenevestigatorQ9SQT8.
GermOnlineAT3G06350. Arabidopsis thaliana.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
3.40.50.720. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR001381. DHquinase_I.
IPR016040. NAD(P)-bd_dom.
IPR011342. Shikimate_DH.
IPR013708. Shikimate_DH-bd_N.
IPR022893. Shikimate_quinate_DH.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamPF01487. DHquinase_I. 1 hit.
PF01488. Shikimate_DH. 1 hit.
PF08501. Shikimate_dh_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01093. aroD. 1 hit.
TIGR00507. aroE. 1 hit.
PROSITEPS01028. DEHYDROQUINASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9SQT8.

Entry information

Entry nameDHQSD_ARATH
AccessionPrimary (citable) accession number: Q9SQT8
Secondary accession number(s): Q3ZLP7, Q56ZH7, Q6NLY1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: May 1, 2000
Last modified: May 1, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents