A0A6S6QLX9 · PLE2_RHOPP
- ProteinAcetyltransferase ple2
- Geneple2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids377 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Acetyltransferase; part of the gene cluster that mediates the biosynthesis of pleuromutilin, a tricyclic diterpene showing antibacterial properties (PubMed:28924980).
The geranylgeranyl diphosphate (GGPP) synthase ple4 catalyzes the first step in pleuromutilin biosynthesis (PubMed:28924980).
GGPP is then substrate of the premutilin synthase (PS) ple3 to yield premutilin (PubMed:28924980).
Premutilin synthase is a bifunctional enzyme composed of the fusion of a class II diterpene cyclase (DTC) and a class I diterpene synthase (DTS), with the corresponding domains and active sites containing characteristic aspartate-rich motifs (By similarity).
GGPP is first converted to mutildienyl-diphosphate (MPP) at the class II DTC site (By similarity).
MPP is subsequently further cyclized at the class I DTS site, followed by a 1,5-hydride shift and addition of water prior to terminating deprotonation, to yield premutilin (By similarity).
The cytochrome P450 monooxygenases ple5 and ple6 hydroxylate premutilin at C-11 and C-3, respectively, producing 11-hydroxypremutilin and 3-hydroxypremutilin (PubMed:28924980).
The combination of the actions of both ple5 and ple6 leads to the production of 3,11-dihydroxypremutilin (PubMed:28924980).
The short chain dehydrogenase ple7 further converts 3,11-dihydroxypremutilin into mutilin (PubMed:28924980).
The acetyltransferase ple2 then acetylates mutilin to produce 14-O-acetylmutilin (PubMed:28924980).
Finally, the cytochrome P450 monooxygenase ple1 catalyzes hydroxylation on the alpha position of the acetyl side chain of 14-O-acetylmutilin to yield pleuromutilin (PubMed:28924980).
The geranylgeranyl diphosphate (GGPP) synthase ple4 catalyzes the first step in pleuromutilin biosynthesis (PubMed:28924980).
GGPP is then substrate of the premutilin synthase (PS) ple3 to yield premutilin (PubMed:28924980).
Premutilin synthase is a bifunctional enzyme composed of the fusion of a class II diterpene cyclase (DTC) and a class I diterpene synthase (DTS), with the corresponding domains and active sites containing characteristic aspartate-rich motifs (By similarity).
GGPP is first converted to mutildienyl-diphosphate (MPP) at the class II DTC site (By similarity).
MPP is subsequently further cyclized at the class I DTS site, followed by a 1,5-hydride shift and addition of water prior to terminating deprotonation, to yield premutilin (By similarity).
The cytochrome P450 monooxygenases ple5 and ple6 hydroxylate premutilin at C-11 and C-3, respectively, producing 11-hydroxypremutilin and 3-hydroxypremutilin (PubMed:28924980).
The combination of the actions of both ple5 and ple6 leads to the production of 3,11-dihydroxypremutilin (PubMed:28924980).
The short chain dehydrogenase ple7 further converts 3,11-dihydroxypremutilin into mutilin (PubMed:28924980).
The acetyltransferase ple2 then acetylates mutilin to produce 14-O-acetylmutilin (PubMed:28924980).
Finally, the cytochrome P450 monooxygenase ple1 catalyzes hydroxylation on the alpha position of the acetyl side chain of 14-O-acetylmutilin to yield pleuromutilin (PubMed:28924980).
Pathway
Secondary metabolite biosynthesis; terpenoid biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Molecular Function | O-acyltransferase activity | |
Biological Process | terpenoid biosynthetic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAcetyltransferase ple2
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Agaricomycetidae > Agaricales > Tricholomatineae > Entolomataceae > Rhodocybe
Accessions
- Primary accessionA0A6S6QLX9
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 29-49 | Helical | ||||
Sequence: WILWVIIVALNTYLTMTTTGD | ||||||
Transmembrane | 56-76 | Helical | ||||
Sequence: IANNLFVITLTATDYILLTDV | ||||||
Transmembrane | 176-196 | Helical | ||||
Sequence: IAAWLLFTTNQVSILLTALSL | ||||||
Transmembrane | 258-278 | Helical | ||||
Sequence: PALYVQLYAAFFLSGVLHAIG |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-27 | |||||
Sequence: MKPFSPELLVLSFILLVLSCAIRPAKG | ||||||
Chain | PRO_5028296751 | 28-377 | Acetyltransferase ple2 | |||
Sequence: RWILWVIIVALNTYLTMTTTGDSTLDYDIANNLFVITLTATDYILLTDVQRELQFRNQKGVEQASLLERIKWATWLVQSRRGVGWNWEPKIFVHRFSPKTSRLSFLLQQLVTGARHYLICDLVSLYSRSPVAFAEPLASRPLIWRCADIAAWLLFTTNQVSILLTALSLMQVLSGYSEPQDWVPVFGRWRDAYTVRRFWGRSWHQLVRRCLSSPGKYLSTKVLGLKPGSNPALYVQLYAAFFLSGVLHAIGDFKVHEDWYKAGTMEFFCVQAVIIQMEDGVLWVGRKLGIKETWYWRALGHLWTVAWFVYSCPNWLGATISGRGKASMALESSLVLGLYRGEWHPPRVAQ |
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length377
- Mass (Da)43,171
- Last updated2020-12-02 v1
- Checksum06AD422A1E07C484