Structure of PDB 1dqs Chain A

Receptor sequence
>1dqsA (length=381) Species: 162425 (Aspergillus nidulans) [Search protein sequence]
PTKISILGRESIIADFGLWRNYVAKDLISDCSSTTYVLVTDTNIGSIYTP
SFEEAFRKRAAEITPSPRLLIYNRPPGEVSKSRQTKADIEDWMLSQNPPC
GRDTVVIALGGGVIGDLTGFVASTYMRGVRYVQVPTTLLAMVDSSIGGKT
AIDTPLGKNLIGAIWQPTKIYIDLEFLETLPVREFINGMAEVIKTAAISS
EEEFTALEENAETILKAVRRRFEGTEEILKARILASARHKAYVVSADERE
GGLRNLLNWGHSIGHAIEAILTPQILHGECVAIGMVKEAELARHLGILKG
VAVSRIVKCLAAYGLPTSLKDARIRKLTAGKHCSVDQLMFNMALDKKNDG
PKKKIVLLSAIGTPYETRASVVANEDIRVVL
3D structure
PDB1dqs Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R130 K152 E194 K250 E260 R264 N268 H271 H275 H287
Catalytic site (residue number reindexed from 1) R127 K149 E191 K240 E250 R254 N258 H261 H265 H277
Enzyme Commision number 1.1.1.25: shikimate dehydrogenase (NADP(+)).
2.5.1.19: 3-phosphoshikimate 1-carboxyvinyltransferase.
2.7.1.71: shikimate kinase.
4.2.1.10: 3-dehydroquinate dehydratase.
4.2.3.4: 3-dehydroquinate synthase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003856 3-dehydroquinate synthase activity
GO:0016838 carbon-oxygen lyase activity, acting on phosphates
Biological Process
GO:0009073 aromatic amino acid family biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1dqs, PDBe:1dqs, PDBj:1dqs
PDBsum1dqs
PubMed9685163
UniProtP07547|ARO1_EMENI Pentafunctional AROM polypeptide (Gene Name=aromA)

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