UniProtKB - A0A1V6PBT1 (CALF_PENDC)
Protein
Bifunctional decalin synthase calF
Gene
calF
Organism
Penicillium decumbens
Status
Functioni
Bifunctional decaline synthase; part of the gene cluster that mediates the biosynthesis of calbistrin A and related compounds. Calbistrin A is a secondary metabolite with an interesting structure that was recently found to have bioactivity against leukemia cells. It consists of two polyketides linked by an ester bond: a bicyclic decalin containing polyketide and a linear 12 carbon dioic acid structure (PubMed:30598828). The polyketide synthase calA is probably responsible for forming the decalin moiety. Because calA lacks a designated enoylreductase (ER) domain, the required activity is provided by the trans-enoyl reductase calK (PubMed:30598828). Following release from the PKS, calF then probably catalyzes the oxidation and the subsequent Diels Alder cycloisomerization that lead to the formation of the decalin moiety (Probable). The decalin polyketide backbone includes two C-methyl groups, at C7 and C11 in backbone, of which the C7 position is probably methylated by the methyltransferase domain of calA. A candidate for adding the methyl group at C11, if not done by CalA, is the cluster methyltransferase calH (Probable). Several additional tailoring enzymes within the cluster could be involved in the modification of the decalin polyketide product. Those include the 3 cytochrome P450 monooxygenases CalE, CalG and CalL, of which one might be responsible for the introduction of the extra hydroxyl group attached to the backbone of the decalin moiety, at position C9 in the backbone, that allows for attachment of the linear moiety (Probable). One tailoring enzyme activity that is expected to be involved in biosynthesis of calbistrin is an acyltransferase for connecting the two polyketide synthase products, and which could be performed by the cluster acyltransferase calJ (Probable). The enzyme responsible for the biosynthesis of the linear moiety, probably a second PKS, has not been identified yet (Probable).1 Publication1 Publication
: Secondary metabolite biosynthesis Pathwayi
This protein is involved in Secondary metabolite biosynthesis.1 PublicationView all proteins of this organism that are known to be involved in Secondary metabolite biosynthesis.
GO - Molecular functioni
- FAD binding Source: InterPro
- isomerase activity Source: UniProtKB-KW
- oxidoreductase activity Source: UniProtKB-KW
Keywordsi
Molecular function | Isomerase, Oxidoreductase |
Ligand | FAD, Flavoprotein |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:calF1 Publication ORF Names:PENDEC_c013G03789 |
Organismi | Penicillium decumbens |
Taxonomic identifieri | 69771 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Penicillium |
Proteomesi |
|
Pathology & Biotechi
Biotechnological usei
Calbistrin A has been reported to possess a number of interesting bioactivities including antifungal active against Candida albicans and cytotoxic toward both healthy and leukemic human cells.2 Publications
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 18 | Sequence analysisAdd BLAST | 18 | |
ChainiPRO_5013206725 | 19 – 575 | Bifunctional decalin synthase calFAdd BLAST | 557 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 46 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Glycosylationi | 103 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Glycosylationi | 127 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Glycosylationi | 175 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Glycosylationi | 268 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Glycosylationi | 308 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Glycosylationi | 359 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Glycosylationi | 425 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Glycosylationi | 485 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 |
Keywords - PTMi
GlycoproteinExpressioni
Inductioni
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 118 – 297 | FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST | 180 |
Sequence similaritiesi
Belongs to the oxygen-dependent FAD-linked oxidoreductase family.Curated
Keywords - Domaini
SignalPhylogenomic databases
OrthoDBi | 827142at2759 |
Family and domain databases
InterProi | View protein in InterPro IPR012951 BBE IPR016166 FAD-bd_PCMH IPR036318 FAD-bd_PCMH-like_sf IPR006094 Oxid_FAD_bind_N |
Pfami | View protein in Pfam PF08031 BBE, 1 hit PF01565 FAD_binding_4, 1 hit |
SUPFAMi | SSF56176 SSF56176, 1 hit |
PROSITEi | View protein in PROSITE PS51387 FAD_PCMH, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
A0A1V6PBT1-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSFKPLLLSL SLLSPALGVA PRQSASCRAI PGDPEWPSTS AWNALNNTVH
60 70 80 90 100
GRLKATVPLP SVCHHEPFGT YNEDACTALK TEWLDDRTFL NNAAEVMNPG
110 120 130 140 150
TQNYSCVPFT SPSQPCQLGN YASYSINVTG ADDVIAGIRF ARQKNIRLVI
160 170 180 190 200
KNTGHDFAGK STGTGALSLW THHLNTTEII SSYESAEYTG PAAKLGAGVI
210 220 230 240 250
SGNVYQVVAE AGYRVMGGTC PTVGLAGGYT SGAGHSLLNG AYGMAADAVL
260 270 280 290 300
EWEVVTAQGE HLIASQSNNT DLYWALSGGG PGTFAVVLSM TTKVFQDGPI
310 320 330 340 350
GSGIMLFNLT SDNTEEYWGA IEDLWAFLPE FVDAGPNTWD FALTSTGFQA
360 370 380 390 400
YAITVPDQNG TQVKSLLQPW LDSIEKRGIQ YSYTPTDSPN YLQYFSSRFG
410 420 430 440 450
PGIAGAGPAT VQLASRLIPR AAMYNATQKK VIVSALRAFI EDGEDLELGC
460 470 480 490 500
HALNVGNIEH PGNAVLPAWR NAIATCNVVN YWDWNITATE MQARKDLLVD
510 520 530 540 550
RLIPGLEEAT PGSGTYLNEI DARWKGDWIT ELYGDNYDRL LQIKNKYDPE
560 570
HRFYAWTAVG SDSWFTDGSG RLCRV
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | MDYL01000013 Genomic DNA Translation: OQD73976.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | MDYL01000013 Genomic DNA Translation: OQD73976.1 |
3D structure databases
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Phylogenomic databases
OrthoDBi | 827142at2759 |
Family and domain databases
InterProi | View protein in InterPro IPR012951 BBE IPR016166 FAD-bd_PCMH IPR036318 FAD-bd_PCMH-like_sf IPR006094 Oxid_FAD_bind_N |
Pfami | View protein in Pfam PF08031 BBE, 1 hit PF01565 FAD_binding_4, 1 hit |
SUPFAMi | SSF56176 SSF56176, 1 hit |
PROSITEi | View protein in PROSITE PS51387 FAD_PCMH, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | CALF_PENDC | |
Accessioni | A0A1V6PBT1Primary (citable) accession number: A0A1V6PBT1 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 10, 2019 |
Last sequence update: | June 7, 2017 | |
Last modified: | November 13, 2019 | |
This is version 16 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Complete proteome, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families - PATHWAY comments
Index of metabolic and biosynthesis pathways