A0A8F4NUY3 · GKAC_PENCI
- ProteinTrans-enoyl reductase gkaC
- GenegkaC
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids361 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Trans-enoyl reductasee; part of the gene cluster that mediates the biosynthesis of GKK1032, fungal natural products containing a macrocyclic para-cyclophane connected to a decahydrofluorene ring system that show potent antitumor activities (PubMed:33834778).
Within the pathway, the PKS-NRPS gkaA, with the help of the trans-enoyl reductase gkaC, synthesize the polyketide-tyrosyl acyl thioester product which can be reductively off-loaded by the terminal reductase (R) domain in gkaA (PubMed:33834778).
The PKS module of gkaA acts in combination with the trans-acting enoyl reductase gkaC to produce a methylated polyketide attached to the ACP domain (PubMed:33834778).
In parallel, the adenylation (A) domain of the NRPS module activated L-tyrosine, which is then transferred to the ACP domain. The condensation (C) domain subsequently links this group to the polyketide chain, forming an enzyme-bound amide (PubMed:33834778).
The alpha/beta hydrolase gkaG is then required to catalyze the subsequent Knoevenagel condensation that affords the 3-pyrrolin-2-one ring, whereas the three proteins gkaB, gkadX and gkaZ then function synergistically to form the cyclophane (Probable)
Within the pathway, the PKS-NRPS gkaA, with the help of the trans-enoyl reductase gkaC, synthesize the polyketide-tyrosyl acyl thioester product which can be reductively off-loaded by the terminal reductase (R) domain in gkaA (PubMed:33834778).
The PKS module of gkaA acts in combination with the trans-acting enoyl reductase gkaC to produce a methylated polyketide attached to the ACP domain (PubMed:33834778).
In parallel, the adenylation (A) domain of the NRPS module activated L-tyrosine, which is then transferred to the ACP domain. The condensation (C) domain subsequently links this group to the polyketide chain, forming an enzyme-bound amide (PubMed:33834778).
The alpha/beta hydrolase gkaG is then required to catalyze the subsequent Knoevenagel condensation that affords the 3-pyrrolin-2-one ring, whereas the three proteins gkaB, gkadX and gkaZ then function synergistically to form the cyclophane (Probable)
Pathway
Mycotoxin biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 48-51 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: CDWK | ||||||
Binding site | 172-175 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SSAS | ||||||
Binding site | 195-198 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SPKN | ||||||
Binding site | 213 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 260-261 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: FE | ||||||
Binding site | 351-352 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: IS |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | nucleotide binding | |
Molecular Function | oxidoreductase activity, acting on NAD(P)H |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTrans-enoyl reductase gkaC
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Penicillium
Accessions
- Primary accessionA0A8F4NUY3
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000458425 | 1-361 | Trans-enoyl reductase gkaC | |||
Sequence: MDSLPTSQRAVVQSEDVGSFEISRGRPIPVPSSSQILIKVFAVALNHCDWKMPARVPCPGTVDGADYSGTIIALGDTAALTSGFKIGDRVAGAQMASQRRRPWVGAFTEYILEEADSAWLVPDSLSWEEAAAIGCAATSSVGMALWKSLNLPGTPQNPITEDGKYVLVYGGSSASGTFAIQLLRLSGYNVVTTCSPKNFGLVESYGAEKAFDYHSPTCGEDIRTYTGNTLEYALDIITEAKTIRHCYAAIGRGGGRYCGFELLPHDLIATMRRSVKAEWVNGLEMTGLEIDLPGGYYCKANPELHIWFADLIKQYSVLISQGKLRPHPIQINKGGLEKVIDGLGQMKRREISGKKMVYPLV |
Interaction
Subunit
Monomer.
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 15-357 | Enoyl reductase (ER) | ||||
Sequence: EDVGSFEISRGRPIPVPSSSQILIKVFAVALNHCDWKMPARVPCPGTVDGADYSGTIIALGDTAALTSGFKIGDRVAGAQMASQRRRPWVGAFTEYILEEADSAWLVPDSLSWEEAAAIGCAATSSVGMALWKSLNLPGTPQNPITEDGKYVLVYGGSSASGTFAIQLLRLSGYNVVTTCSPKNFGLVESYGAEKAFDYHSPTCGEDIRTYTGNTLEYALDIITEAKTIRHCYAAIGRGGGRYCGFELLPHDLIATMRRSVKAEWVNGLEMTGLEIDLPGGYYCKANPELHIWFADLIKQYSVLISQGKLRPHPIQINKGGLEKVIDGLGQMKRREISGKKMV |
Sequence similarities
Belongs to the zinc-containing alcohol dehydrogenase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length361
- Mass (Da)39,162
- Last updated2022-01-19 v1
- ChecksumEBB3B01CCA64CEB1