IED ID |
IndEnz0010001611 |
Enzyme Type ID |
esterase001611 |
Protein Name |
Clavatol biosynthesis cluster protein B
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Gene Name |
claB |
Organism |
Penicillium crustosum (Blue mold fungus) |
Taxonomic Lineage |
cellular organisms
Eukaryota
Opisthokonta
Fungi
Dikarya
Ascomycota
saccharomyceta
Pezizomycotina
leotiomyceta
Eurotiomycetes
Eurotiomycetidae
Eurotiales (green and blue molds)
Aspergillaceae
Penicillium
Penicillium crustosum (Blue mold fungus)
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Enzyme Sequence |
MAALSFQCLCVASAVRAWERIESMVDVSFDVIIAASAQTIQLSQQSQQCQLHSQSSAAEAYNTFIRIYGRLVPLLERAITTYATNLQPPLSTSPTFQRTDPRNLTYPLDNQVLGSVLRDFSTHRSLQEQRNPATMVCRPSKMTLGQYEMDEQQSQYLALDVICRTLRNLVIVLQEMGGGENAEIRQVDARLLTILVQVRRLLENTSATLSILES |
Enzyme Length |
214 |
Uniprot Accession Number |
A0A481WNL0 |
Absorption |
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Active Site |
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Activity Regulation |
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Binding Site |
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Calcium Binding |
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catalytic Activity |
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DNA Binding |
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EC Number |
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Enzyme Function |
FUNCTION: Part of the cla gene cluster that produces clavatol and ortho-quinone methide (PubMed:30811183). The clavatol biosynthesis cluster cla and the terrestric acid cluster tra are both involved in the production of peniphenones and penilactones (PubMed:30811183). The non-reducing PKS claF is responsible for the formation of clavatol from successive condensations of 3 malonyl-CoA units, presumably with a simple acetyl-CoA starter unit, and 2 methylation steps (PubMed:30811183). The esterase claE probably collaborates with claF by catalyzing the hydrolysis of ACP-bound acyl intermediates to free the ACP from stalled intermediates (By similarity). The clavatol oxidase claD then converts clavatol to hydroxyclavatol (PubMed:30811183). Spontaneous dehydration of hydroxyclavatol leads to the accumulation of the highly active ortho-quinone methide (PubMed:30811183, PubMed:31860310). On the other hand, the PKS-NRPS hybrid traA is involved in the formation of crustosic acid, with the help of traB and traD (PubMed:30811183). The polyketide synthase module (PKS) of traA is responsible for the synthesis of the polyketide backbone via the condensation of an acetyl-CoA starter unit with 3 malonyl-CoA units (PubMed:30811183). The downstream nonribosomal peptide synthetase (NRPS) module then amidates the carboxyl end of the polyketide with L-malic acid (PubMed:30811183). Because traA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase traG (By similarity). Crustosic acid undergoes decarboxylation and isomerization to the terrestric acid, catalyzed by the 2-oxoglutarate-dependent dioxygenase traH (PubMed:30811183). Both acids are further converted to the 2 gamma-butyrolactones (R)-5-methyltetronic acid and (S)-5-carboxylmethyltetronic acid, with involvement of the cytochrome P450 monooxygenase claJ (PubMed:30811183). Spontaneous addition of the methide to these gamma-butyrolactones leads to peniphenone D and penilactone D, which undergo again stereospecific attacking by methide to give penilactones A and B (PubMed:30811183, PubMed:31860310). The function of claB has not been investigated yet (Probable). {ECO:0000250|UniProtKB:A0A0E0RXA7, ECO:0000250|UniProtKB:A0A161CKG1, ECO:0000269|PubMed:30811183, ECO:0000269|PubMed:31860310, ECO:0000305|PubMed:30811183}. |
Temperature Dependency |
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PH Dependency |
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Pathway |
PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305|PubMed:30811183}. |
nucleotide Binding |
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Features |
Chain (1); Glycosylation (2); Signal peptide (1) |
Keywords |
Glycoprotein;Signal |
Interact With |
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Induction |
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Subcellular Location |
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Modified Residue |
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Post Translational Modification |
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Signal Peptide |
SIGNAL 1..17; /evidence=ECO:0000255 |
Structure 3D |
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Cross Reference PDB |
- |
Mapped Pubmed ID |
- |
Motif |
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Gene Encoded By |
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Mass |
24,011 |
Kinetics |
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Metal Binding |
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Rhea ID |
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Cross Reference Brenda |
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