Family Search for PF08592 (Anthrone_oxy)
PaperBLAST, GapMind, SitesBLAST, and Sites on a Tree will be down for server maintenance on Friday March 29.
Running HMMer for PF08592
PF08592 hits 24 sequences in PaperBLAST's database above the trusted cutoff. Showing all hits. Or show only hits to curated sequences or try another family.
TPCL_ASPFU / Q4WQY6 Anthrone oxygenase tpcL; Trypacidin synthesis protein L; EC 1.10.3.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see 3 papers)
AFUA_4G14480, Afu4g14480 conserved hypothetical protein from Aspergillus fumigatus Af293
Aligns to 50:153 / 161 (64.6%), covers 100.0% of PF08592, 95.1 bits
- function: Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of trypacidin, a mycotoxin with antiprotozoal activity and that plays a role in the infection process (PubMed:26278536, PubMed:26242966). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) tpcC (PubMed:26242966). The atrochrysone carboxyl ACP thioesterase tpcB then breaks the thioester bond and releases the atrochrysone carboxylic acid from tpcC (PubMed:26242966). The decarboxylase tpcK converts atrochrysone carboxylic acid to atrochrysone which is further reduced into emodin anthrone (PubMed:26242966). The next step is performed by the emodin anthrone oxygenase tpcL that catalyzes the oxidation of emodinanthrone to emodin (PubMed:26242966). Emodin O-methyltransferase encoded by tpcA catalyzes methylation of the 8-hydroxy group of emodin to form questin (PubMed:26242966). Ring cleavage of questin by questin oxidase tpcI leads to desmethylsulochrin via several intermediates including questin epoxide (By similarity). Another methylation step catalyzed by tpcM leads to the formation of sulochrin which is further converted to monomethylsulfochrin by tpcH. Finally, the tpcJ catalyzes the conversion of monomethylsulfochrin to trypacidin (PubMed:26242966). Trypacidin is toxic for human pulmonary and bronchial epithelial cells by initiating the intracellular formation of nitric oxide (NO) and hydrogen peroxide (H(2)O(2)), thus triggering host necrotic cell death (PubMed:22319557). The trypacidin pathway is also able to produce endocrocin via a distinct route from the endocrocin Enc pathway (PubMed:26242966).
catalytic activity: emodin anthrone + O2 = emodin + H(+) + H2O (RHEA:64268) - Temperature during conidiation affects stress tolerance, pigmentation, and trypacidin accumulation in the conidia of the airborne pathogen Aspergillus fumigatus
Hagiwara, PloS one 2017 - “...23.8 33.01 0.25 tpcH hypothetical protein AFUA_8G06890 101.5 3.2 7.3 32.02 2.29 extracellular exo-polygalacturonase, putative AFUA_4G14480 1253.4 40.1 7.5 31.26 0.19 tpcL conserved hypothetical protein AFUA_4G14470 1073.0 34.5 8.5 31.08 0.25 tpcK hypothetical protein AFUA_5G01260 572.4 19.4 6.0 29.54 0.31 ankyrin repeat protein AFUA_4G14560 270.6 9.3...”
- Regulation of Secondary Metabolism by the Velvet Complex Is Temperature-Responsive in Aspergillus
Lind, G3 (Bethesda, Md.) 2016 - “..., Afu4g12050 , Afu4g12060 , Afu4g12070 Inglis et al. (2013) Cluster 20 Trypacidin Afu4g14460 , Afu4g14480 , Afu4g14470 , Afu4g14490 , Afu4g14500 , Afu4g14510 , Afu4g14520 , Afu4g14530 , Afu4g14540 , Afu4g14550 , Afu4g14560 , Afu4g14570 , Afu4g14580 Throckmorton et al. (2015) ; Mattern et al....”
AGN2_PAEDI / A0A411PQQ5 Anthrone oxygenase AgnL2; Agnestins biosynthesis cluster protein L2; EC 1.10.3.- from Paecilomyces divaricatus (Penicillium divaricatum) (see paper)
Aligns to 46:155 / 164 (67.1%), covers 100.0% of PF08592, 90.5 bits
- function: Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of agnestins, dihydroxy-xanthone metabolites (PubMed:30746079). The pathway begins with the assembly and cyclization of atrochrysone thioester by the non-reducing polyketide synthase Agnpks1 (PubMed:30746079). The atrochrysone carboxyl ACP thioesterase AgnL7 then breaks the thioester bond and releases the atrochrysone carboxylic acid as the first enzyme-free intermediate (PubMed:30746079). The decarboxylase AgnL1 then catalyzes the concerted decarboxylation-elimination required to convert atochrysone carboxylic acid into emodin anthrone, which is further oxidized to emodin by the anthrone oxygenase AgnL2 (PubMed:30746079). Emodin then undergoes reduction catalyzed by the oxidoreductase AgnL4 to yield the dihydroquinone tautomer which is the substrate for reduction by the short chain dehydrogenase AgnL6 reduction to produce hydroxyketone, followed by AgnL8 dehydration and likely spontaneous autoxidation to chrysophanol (PubMed:30746079). Baeyer-Villiger oxidation by the oxidase AgnL3 leads to monodictyphenone via cleavage of the C-10/C-10a bond of chrysophanol (PubMed:30746079). Alternative cleavage at the C- 4a/C-10 bond of chrysophanol leads also to the formation some cephalone F (PubMed:30746079). Further conversion to agnestins A and B, requires reduction to dihydro-monodictyphenone, oxidation to agnestin C probably via an epoxide, and rearrangement to either agnestin A or agnestin B directly, although agnestin A or agnestin B can also interconvert (PubMed:30746079). Within the cluster, AgnR1 is the only unassigned oxidoreductase present which could be involved in this conversion. However, AgnR1 seems not to be involved in this step, and thus genes involved in the proposed oxidation/reduction may be located elsewhere on the genome (PubMed:30746079). Further agnestin A derivatives are probably formed by spontaneous decarboxylations, dehydrations and methanolysis reactions (PubMed:30746079).
catalytic activity: emodin anthrone + O2 = emodin + H(+) + H2O (RHEA:64268)
PTAC_PESFW / A0A067XMT5 Anthrone oxygenase ptaC; Pestheic acid biosynthesis cluster protein C; EC 1.-.-.- from Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) (see 2 papers)
Aligns to 26:135 / 141 (78.0%), covers 99.1% of PF08592, 88.2 bits
- function: Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes (PubMed:24302702). The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA (PubMed:24302702). As the ptaA protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization of the polyketide could be catalyzed by ptaB containing a beta-lactamase domain (PubMed:24302702). The ptaB protein might hydrolyze the thioester bond between the ACP of ptaA and the intermediate to release atrochrysone carboxylic acid, which is spontaneously dehydrated to form endocrocin anthrone (PubMed:24302702). Endocrocin anthrone is then converted to endocrocin, catalyzed by the anthrone oxygenase ptaC (PubMed:24302702). Spontaneous decarboxylation of endocrocin occurs to generate emodin (PubMed:24302702). An O- methyltransferase (ptaH or ptaI) could methylate emodin to form physcion (PubMed:24302702). PtaJ could then catalyze the oxidative cleavage of physcion, and rotation of the intermediate could then afford desmethylisosulochrin (PubMed:24302702). PtaF, a putative NADH- dependent oxidoreductase, might also participate in the oxidative cleavage step (PubMed:24302702). Desmethylisosulochrin is then transformed by another O-methyltransferase (ptaH or ptaI) to form isosulochrin (PubMed:24302702). Chlorination of isosulochrin by ptaM in the cyclohexadienone B ring then produces chloroisosulochrin (PubMed:24302702). PtaE is responsible for the oxidative coupling reactions of both benzophenones isosulochrin and chloroisosulochrin to RES-1214-1 and pestheic acid respectively, regardless of chlorination.
HYPC_DOTSN / M2WJF5 Monooxygenase hypC; Dothistromin biosynthesis protein hypC; EC 1.-.-.- from Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight fungus) (Mycosphaerella pini) (see 3 papers)
Aligns to 68:174 / 185 (57.8%), covers 100.0% of PF08592, 87.8 bits
- function: Monooxygenase; part of the fragmented gene cluster that mediates the biosynthesis of dothistromin (DOTH), a polyketide toxin very similar in structure to the aflatoxin precursor, versicolorin B (PubMed:12039746, PubMed:17683963, PubMed:22069571, PubMed:23207690, PubMed:23448391). The first step of the pathway is the conversion of acetate to norsolorinic acid (NOR) and requires the fatty acid synthase subunits hexA and hexB, as well as the polyketide synthase pksA (PubMed:16649078, PubMed:23207690). PksA combines a hexanoyl starter unit and 7 malonyl-CoA extender units to synthesize the precursor NOR (By similarity). The hexanoyl starter unit is provided to the acyl- carrier protein (ACP) domain by the fungal fatty acid synthase hexA/hexB (By similarity). The second step is the conversion of NOR to averantin (AVN) and requires the norsolorinic acid ketoreductase nor1, which catalyzes the dehydration of norsolorinic acid to form (1'S)- averantin (PubMed:23207690). The cytochrome P450 monooxygenase avnA then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN) (PubMed:23207690). The next step is performed by adhA that transforms HAVN to averufin (AVF) (PubMed:23207690). Averufin might then be converted to hydroxyversicolorone by cypX and avfA (PubMed:23207690). Hydroxyversicolorone is further converted versiconal hemiacetal acetate (VHA) by moxY (PubMed:23207690). VHA is then the substrate for the versiconal hemiacetal acetate esterase est1 to yield versiconal (VAL) (PubMed:23207690). Versicolorin B synthase vbsA then converts VAL to versicolorin B (VERB) by closing the bisfuran ring (PubMed:16649078, PubMed:23207690). Then, the activity of the versicolorin B desaturase verB leads to versicolorin A (VERA) (PubMed:23207690). DotB, a predicted chloroperoxidase, may perform epoxidation of the A-ring of VERA (PubMed:23207690). Alternatively, a cytochrome P450, such as cypX or avnA could catalyze this step (PubMed:23207690). It is also possible that another, uncharacterized, cytochrome P450 enzyme is responsible for this step (PubMed:23207690). Opening of the epoxide could potentially be achieved by the epoxide hydrolase epoA (PubMed:23207690). However, epoA seems not to be required for DOTH biosynthesis, but other epoxide hydrolases may have the ability to complement this hydrolysis (PubMed:23207690). Alternatively, opening of the epoxide ring could be achieved non-enzymatically (PubMed:23207690). The next step is the deoxygenation of ring A to yield the 5,8- dihydroxyanthraquinone which is most likely catalyzed by the NADPH dehydrogenase encoded by ver1 (PubMed:23207690). The last stages of DOTH biosynthesis are proposed to involve hydroxylation of the bisfuran (PubMed:23207690). OrdB and norB might have oxidative roles here (PubMed:23207690). An alternative possibility is that cytochrome P450 monoogenases such as avnA and cypX might perform these steps in addition to previously proposed steps (PubMed:23207690).
AFUA_4G09250 conserved hypothetical protein from Aspergillus fumigatus Af293
Aligns to 55:168 / 175 (65.1%), covers 100.0% of PF08592, 86.6 bits
- Genetic Analyses of Amphotericin B Susceptibility in Aspergillus fumigatus
Fan, Journal of fungi (Basel, Switzerland) 2021 - “...eight SNPs, four were on chromosome 4 and were intergenic variants found between AFUA_4G09240 and AFUA_4G09250 . The remaining four SNPs were located on chromosome 5: two were missense variants in AFUA_5G00710 and in AFUA_5G09220 , one was a non-coding transcript variant in AFUA_5G09320 , and...”
- “...were intergenic variants and comprised of four SNPs in the intergenic region between AFUA_4G09240 and AFUA_4G09250 , which both encode for uncharacterized proteins, and one intergenic variant between AFUA_5G00700 and AFUA_5G00710 , encoding for an uncharacterized protein and a putative gamma-aminobutyric acid (GABA) permease, respectively. These...”
- Redundant synthesis of a conidial polyketide by two distinct secondary metabolite clusters in Aspergillus fumigatus
Throckmorton, Environmental microbiology 2016 - “...tpcK is upstream of tpcL in the trypacidin pathway. A third putative anthrone oxidase-encoding gene, AFUA_4G09250, was found in the A. fumigatus genome, however, its deletion had no effect on the levels of metabolites in the endocrocin or trypacidin pathways ( Fig. 5BD; Fig. S7 )....”
- “...trypacidin cluster mutants ( encC , tpcK , tpcL , tpcK/ t pcL , and AFUA_4G09250 (250), BD; encC , tpcK/ encC , tpcL / encC , tpcK/ t pc L/ encC , and AFUA_4G09250/ encC ( 250/ encC ), EG) at 285 nm (B and...”
DMR16_CRYX8 / A0A4P8DK01 Anthrone oxygenase dmxR16; Dimeric xanthone biosynthesis cluster protein R16; EC 1.10.3.- from Cryptosporiopsis sp. (strain 8999) (see paper)
Aligns to 60:160 / 171 (59.1%), covers 100.0% of PF08592, 85.1 bits
- function: Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of the dimeric xanthones cryptosporioptides (PubMed:30996871). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase dmx-nrPKS (Probable). The atrochrysone carboxyl ACP thioesterase dmxR1 then breaks the thioester bond and releases the atrochrysone carboxylic acid from dmx- nrPKS (Probable). Atrochrysone carboxylic acid is decarboxylated by the decarboxylase dmxR15, and oxidized by the anthrone oxygenase dmxR16 to yield emodin (Probable). Emodin is then reduced to emodin hydroquinone by the oxidoreductase dmxR7 (Probable). A-ring reduction by the short chain dehydrogenase dmxR18, dehydration by the scytalone dehydratase- like protein dmxR17 and probable spontaneous re-oxidation, results in overall deoxygenation to chrysophanol (PubMed:30996871). Baeyer- Villiger oxidation by the Baeyer-Villiger monooxygenase (BVMO) dmxR6 then yields monodictylactone in equilibrium with monodictyphenone (PubMed:30996871). In the case of the cryptosporioptides biosynthesis, monodictylactone is reduced at C-12 to an alcohol (by the short chain dehydrogenases dmxR12 or dmxR8) and hydroxylated at C-5 by dmxR9, yielding the electron-rich aromatic which could eliminate H(2)O to form the ortho-quinonemethide, followed by tautomerisation to paraquinone and complete the formal reduction to produce the 10-methylgroup (Probable). Conjugate addition of C-4a-OH to the resulting paraquinone by the monooxygenase dmxR10 then gives cyclohexadienone, which is then reduced at C-5 by the short chain dehydrogenase dmxR3 to give the dihydroxanthone (Probable). The 6,7-epoxide in the cryptosporioptides could be introduced by the cytochrome P450 monooxygenase dmxL3 (Probable). The highly reducing PKS dmxL2 manufactures butyrate, which is further carboxylated by dmxL1 to form ethylmalonate (PubMed:30996871). It is not yet clear whether the carboxylation occurs while the butyrate is attached to the ACP of dmxL2, but this unusual fungal metabolite could then be esterified to O-5 by the O- acetyltransferase dmxR13 (PubMed:30996871). Finally, dimerization performed by dmxR5 gives the observed dimers cryptosporioptides A, B and C as the final products of the pathway (PubMed:30996871).
catalytic activity: emodin anthrone + O2 = emodin + H(+) + H2O (RHEA:64268)
PK81C_PSEFD / M3APK4 Anthrone oxygenase MYCFIDRAFT_34418; PKS8-1 gene cluster protein MYCFIDRAFT_34418; EC 1.10.3.- from Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease fungus) (Mycosphaerella fijiensis) (see 2 papers)
Aligns to 56:159 / 173 (60.1%), covers 100.0% of PF08592, 84.9 bits
- function: Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of an emodin derivative that may be involved in black Sigatoka disease of banana (PubMed:27388157, PubMed:30735556). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase PKS8-1 (Probable). The atrochrysone carboxyl ACP thioesterase MYCFIDRAFT_190111 then breaks the thioester bond and releases the atrochrysone carboxylic acid from PKS8-1 (Probable). The decarboxylase MYCFIDRAFT_34057 then catalyzes the concerted decarboxylation-elimination required to convert atochrysone carboxylic acid into emodin anthrone, which is further oxidized to emodin by the anthrone oxygenase MYCFIDRAFT_34418 (Probable). The functions of the other tailoring enzymes as well as the final product of the cluster have still to be identified (Probable).
catalytic activity: emodin anthrone + O2 = emodin + H(+) + H2O (RHEA:64268)
PIG13_CLAP2 / M1VWN5 Anthrone oxygenase CPUR_05435; Ergochrome gene cluster protein CPUR_05435; EC 1.10.3.- from Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum) (see 2 papers)
Aligns to 50:157 / 174 (62.1%), covers 100.0% of PF08592, 84.7 bits
- function: Anthrone oxygenase; part of the ergochrome gene cluster responsible for the typical purple-black color of the ergot sclerotia (PubMed:28955461). The ergochrome gene cluster produces several ergot pigments including the yellow ergochrome secalonic acid and its derivatives, as well as the red anthraquinones endocrocin and clavorubin (PubMed:28955461). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) CPUR_05437 (By similarity). The atrochrysone carboxyl ACP thioesterase CPUR_05436 then breaks the thioester bond and releases the atrochrysone carboxylic acid from CPUR_05437 (By similarity). The decarboxylase CPUR_05434 then catalyzes the concerted decarboxylation-elimination required to convert atochrysone carboxylic acid into emodin anthrone, which is further oxidized to emodin by the anthrone oxygenase CPUR_05435 (By similarity). Emodin is further modified to yield monodictyphenone via several steps involving CPUR_05427, CPUR_05428, CPUR_05429 and CPUR_05430 (By similarity). The short chain dehydrogenase/reductase CPUR_05418 then catalyzes the C-5 ketoreduction to give the xanthone skeleton of the monomeric units (PubMed:32105084). Ergochromes formation requires further dimerization steps of different xanthone units, probably catalyzed by the cytochrome P450 monooxygenase CPUR_05419 (PubMed:28955461). CPUR_05425, CPUR_05426 and CPUR_05431 are unique to Claviceps, thus it is likely that they are involved in further modification of xanthone units or in their dimerization (PubMed:28955461). The yellow ergochromes and the red anthraquinone pigments endocrocin and clavorubin are products from the same PKS derived precursors and the latter are likely shunt products in the pathway of xanthone biosynthesis (PubMed:28955461). It is proposed that atrochrysone carboxylic acid released from the PKS CPUR_05437 can also be converted to endocrocin anthrone which is further oxidized into endocrocin by CPUR_05435 (By similarity). Endocrocin could be then modified to clavorubin, possibly by CPUR_05423 and CPUR_05431 (PubMed:28955461). Clavorubin is the principal anthraquinone metabolite produced by the cluster with a much higher yield compared to endocrocin (PubMed:28955461).
catalytic activity: emodin anthrone + O2 = emodin + H(+) + H2O (RHEA:64268)
AO090023000611 No description from Aspergillus oryzae RIB40
Aligns to 55:169 / 182 (63.2%), covers 100.0% of PF08592, 83.5 bits
ENCC_ASPFU / A4DA85 Anthrone oxygenase encC; Endocrocin synthesis protein C; EC 1.-.-.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see 4 papers)
AFUA_4G00225 conserved hypothetical protein from Aspergillus fumigatus Af293
Aligns to 52:168 / 181 (64.6%), covers 100.0% of PF08592, 81.2 bits
- function: Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of endocrocin, a simple anthraquinone interesting for many biotechnological applications (PubMed:22492455, PubMed:23592999). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) encA (PubMed:22492455). The atrochrysone carboxyl ACP thioesterase encB then breaks the thioester bond and releases the atrochrysone carboxylic acid from encA (PubMed:22492455). The atrochrysone carboxylic acid is then converted to endocrocin anthrone which is further oxidized into endocrocin by the anthrone oxygenase encC (PubMed:22492455). The exact function of encD has not been identified yet, but it negatively regulates endocrocin production, likely through the modification of endocrocin itself (PubMed:22492455).
disruption phenotype: Leads to unstable anthrone production and abolishes the production of endocrocin (PubMed:22492455). - Genomes and secretomes of Ascomycota fungi reveal diverse functions in plant biomass decomposition and pathogenesis
Challacombe, BMC genomics 2019 - “...identity to the query sequence, and the conserved hypothetical protein in the endocrocin gene cluster (AFUA_4G00225, 34% identity). The hits to all of the A. fumigatus Af293 query sequences are listed in Additional file 18 Aspergillus SMs tab. The high % identity hits matching each A....”
- Genome-based cluster deletion reveals an endocrocin biosynthetic pathway in Aspergillus fumigatus
Lim, Applied and environmental microbiology 2012 - “...the endocrocin cluster genes (2). Protein sequence alignment of AFUA_4G00225 (EncC) to HypC and other related proteins was done using the Clustal W method (42)...”
- “...this ORF was annotated in the CADRE site as AFUA_4G00225 (28). As shown in Fig. 3, mRNA supported the existence of this ORF. Additionally, a PSI-BLAST search...”
gedH / P0DOB2 anthrone oxygenase from Aspergillus terreus (strain NIH 2624 / FGSC A1156) (see paper)
GEDH_ASPTN / P0DOB2 Anthrone oxygenase gedH; Geodin synthesis protein H; EC 1.10.3.- from Aspergillus terreus (strain NIH 2624 / FGSC A1156) (see 7 papers)
Aligns to 34:136 / 150 (68.7%), covers 100.0% of PF08592, 78.8 bits
- function: Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of geodin, an intermediate in the biosynthesis of other natural products (PubMed:7665560, PubMed:19549600, PubMed:24009710). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) gedC (PubMed:12536215, PubMed:19549600). The atrochrysone carboxyl ACP thioesterase gedB then breaks the thioester bond and releases the atrochrysone carboxylic acid from gedC (PubMed:19549600). The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone (PubMed:24009710). The next step is performed by the emodin anthrone oxygenase gedH that catalyzes the oxidation of emodinanthrone to emodin (PubMed:1810248). Emodin O-methyltransferase encoded probably by gedA then catalyzes methylation of the 8-hydroxy group of emodin to form questin (PubMed:1444712). Ring cleavage of questin by questin oxidase gedK leads to desmethylsulochrin via several intermediates including questin epoxide (PubMed:3182756). Another methylation step probably catalyzed by methyltransferase gedG leads to the formation of sulochrin which is further converted to dihydrogeodin by the sulochrin halogenase gedL (PubMed:24009710). Finally, the dihydrogeodin oxidase gedJ catalyzes the stereospecific phenol oxidative coupling reaction converting dihydrogeodin to geodin (PubMed:7665560).
catalytic activity: emodin anthrone + O2 = emodin + H(+) + H2O (RHEA:64268) - Characterisation of the biosynthetic pathway to agnestins A and B reveals the reductive route to chrysophanol in fungi
Szwalbe, Chemical science 2019 - “...32 agnL3 BVMO CPUR_05427, M1WG92 (51) MdpL, (42) GedK, (43) 33 agnL2 Anthrone oxidase GedH, P0DOB2 (46) MdpH2, (43) GedH, (46) 34 agnL1 Decarboxylase TpcK, Q4WQY7 (72) MdpH1, (59) GedI, (67) agnPKS nr-PKS MdpG, Q5BH30 (66) MdpG, (66) GedC, (65) 35 agnR1 Oxidoreductase The proposed agn...”
NSRD_ASPN1 / A0A2I1C3V3 Anthrone oxygenase nsrD; Neosartorin biosynthesis cluster protein D; EC 1.10.3.- from Aspergillus novofumigatus (strain IBT 16806) (see 3 papers)
Aligns to 47:151 / 162 (64.8%), covers 99.1% of PF08592, 76.7 bits
- function: Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of the tetrahydroxanthone dimer neosartorin, which exhibits antibacterial activity (PubMed:30394754, PubMed:32105084, PubMed:33891392). The two different monomeric units appear to be synthesized by the same set of enzymes, among which the Baeyer-Villiger monooxygenase nsrF is the key enzyme for the divergence of the biosynthetic routes (PubMed:32105084). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase nsrB (PubMed:32105084). The atrochrysone carboxyl ACP thioesterase nsrC then breaks the thioester bond and releases the atrochrysone carboxylic acid from AacuL (PubMed:32105084). Atrochrysone carboxylic acid is decarboxylated by the decarboxylase nsrE, and oxidized by the anthrone oxygenase nsrD to yield emodin (PubMed:32105084). Emodin is then reduced to emodin hydroquinone by the oxidoreductase nsrR (PubMed:32105084). A-ring reduction by the short chain dehydrogenase nsrJ, dehydration by the scytalone dehydratase-like protein nsrI and probable spontaneous re-oxidation, results in overall deoxygenation to chrysophanol (PubMed:32105084). The Baeyer-Villiger monooxygenase nsrF accepts chrysophanol as a substrate to insert one oxygen atom at two different positions to yield the precursors of both monomric units (PubMed:30394754, PubMed:32105084, PubMed:33891392). NsrF is promiscuous/flexible in interacting with the 2 (non methylated and methylated) aromatic rings of chrysophanol, thus diverging the biosynthetic pathway at this point (PubMed:30394754, PubMed:32105084, PubMed:33891392). After the hydrolysis of the lactones, methylesterification by the methyltransferase nsrG yields respectively moniliphenone and 2,2',6'-trihydroxy-4-methyl-6-methoxya- cyldiphenylmethanone (PubMed:30394754, PubMed:32105084). The next steps are the hydroxylation by the FAD-dependent monooxygenase nsrK, followed by isomerization by the monooxygenase nsrQ (PubMed:32105084). The short chain dehydrogenase/reductase nsrO then catalyzes the C-5 ketoreduction to give the xanthone skeleton of blennolide C and 5-acetylblennolide A (PubMed:32105084). The acetyltransferase nsrL has a strict substrate specificity and uses only blennolide A but not blennolide C to yield 5- acetylblennolide A as the single-acetylated product (PubMed:30394754). In the final step of the biosynthesis, the heterodimerization of the 2 xanthones, blennolide C and 5-acetylblennolide A, is catalyzed by the cytochrome P450 monooxygenase nsrP (PubMed:30394754). NsrP can utilize at least three different xanthones as its substrates to perform the dimerization reaction (PubMed:30394754).
catalytic activity: emodin anthrone + O2 = emodin + H(+) + H2O (RHEA:64268)
HYPC_ASPFN / B8NI03 Noranthrone monooxygenase; EC 1.13.12.20 from Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) (see paper)
Aligns to 92:199 / 210 (51.4%), covers 100.0% of PF08592, 72.9 bits
- function: Monooxygenase that converts norsolorinic acid anthrone to norsolorinic acid during aflatoxin biosynthesis.
catalytic activity: noranthrone + O2 = H2O + norsolorinic acid (RHEA:35191)
disruption phenotype: Cells accumulate excess amounts of norsolorinic acid (NA) and a small amount of norsolorinic acid anthrone (NAA).
An04g04280 uncharacterized protein from Aspergillus niger
Aligns to 58:174 / 181 (64.6%), covers 100.0% of PF08592, 72.8 bits
MDPH2_EMENI / P9WEV9 Anthrone oxygenase; Monodictyphenone synthesis protein H-2; EC 1.10.3.- from Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) (see 3 papers)
Aligns to 47:186 / 192 (72.9%), covers 100.0% of PF08592, 68.8 bits
- function: Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative (PubMed:20139316, PubMed:21351751, PubMed:22730213). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG (PubMed:20139316). The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioester bond and releases the atrochrysone carboxylic acid from mdpG (PubMed:20139316). The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone by mdpH-1 and mdpH-2 (PubMed:20139316). Emodin is further modified to yield monodictyphenone via several steps involving mdpB, mdpC mdpJ, mdpK and mdpL (PubMed:20139316, PubMed:21351751). These enzymes with xptA, xptB and xptC are also proposed to be involved in the synthesis of shamixanthone from emodin (PubMed:22730213). Especially, direct reduction of emodin by the short chain dehydrogenase mdpC followed by dehydration catalyzed by the scytalone dehydratase-like protein mdpB gives loss of oxygen and formation of chrysophanol intermediate in two simple steps (PubMed:22730213).
catalytic activity: emodin anthrone + O2 = emodin + H(+) + H2O (RHEA:64268)
disruption phenotype: Impairs the production of monodictyphenone, but leads to the accumulation of endocrocin (PubMed:20139316, PubMed:21351751).
FRAAL1789 hypothetical protein from Frankia alni ACN14a
Aligns to 47:142 / 162 (59.3%), covers 91.5% of PF08592, 68.3 bits
IW22_14850 anthrone oxygenase family protein from Chryseobacterium sp. JM1
Aligns to 54:150 / 163 (59.5%), covers 98.1% of PF08592, 65.6 bits
Q82D63 Membrane protein from Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
Aligns to 60:157 / 184 (53.3%), covers 99.1% of PF08592, 60.6 bits
- On the Regularities of the Polar Profiles of Proteins Related to Ebola Virus Infection and their Functional Domains.
Polanco, Cell biochemistry and biophysics 2018 - “...PIM HPIEV REVP 1 RND183 DICYDQHVPRYDTVYTRQCSPECTHLACADICVVEESQDHFFIPIIQWIFMDIWNLKILTFEVYQVRGPPGEWWRFLSYIAIADDFETIMMQGFKDYWMATKDPPEWKFAAINLHQELAQGVDEGYQYRSPGLAVFAEILRHDKMNMEQLYHTSCEKKHWMNYKQTWAGPMSDWVEQNA Q6T5A6 511 F5YCB6 1225 B6WUY2 2638 31, 32, 36 Q82D63 3962 43 63100 101145 146179 2 RND220 LDKTTAEAYQPHHVERKHYKLGEPHRECQYWEGEKTVEIDKKSTDGFLLGQCAAAFISELRGDAIVRPEKYYIDEHQRYIDHERPDGYHDIAKGGEEVSRQERGHFESCHKDSRRSQVRQLAIVRWSKQWGQEDMDGKHEFSYGMDTREQDCREKRRDIGYGYHDYCEMCHPQDDKRKGACDKSQVDCFWFIIEHKMYEIEKTQCYSRHRRVHHYDHRDV A0A0N4T4W1 613 A0A0L0BSB2 1419 M1UHL8 2030 3138 A0A0L7RF30 3950 42, 45 A0A151WQ76 5159 52 G7KUA6 6071 60, 68 A0A0R3RF70 7279 A0A0R3RF69 8087...”
SPO1054 anthrone oxygenase family protein from Ruegeria pomeroyi DSS-3
Aligns to 51:153 / 169 (60.9%), covers 99.1% of PF08592, 59.5 bits
SPBC800.14c DUF1772 family protein from Schizosaccharomyces pombe
Aligns to 45:152 / 160 (67.5%), covers 99.1% of PF08592, 57.9 bits
- Dataset describing the genome wide effects on transcription resulting from alterations in the relative levels of the bZIP transcription factors Atf1 and Pcr1 in Schizosaccharomyces pombe
Basu, Data in brief 2022 - “...flavin oxidoreductase, implicated in cellular detoxification from family members SPAC3G6.13c rpl4101 60S ribosomal protein L41 SPBC800.14c SPBC800.14c mitochondrial DUF1772 family protein, multimembrane spanning anthrone oxygenase-like SPCC191.01 SPCC191.01 Schizosaccharomyces specific protein, uncharacterized SPBC4B4.05 smg1 Sm snRNP core protein Smg1 SPAC922.04 SPAC922.04 Schizosaccharomyces specific protein, uncharacterized SPAPJ691.03 mic10...”
- Discovery of genes involved in mitosis, cell division, cell wall integrity and chromosome segregation through construction of Schizosaccharomyces pombe deletion strains
Chen, Yeast (Chichester, England) 2016 - “...gene deletion strains were generated previously: SPAC23C4.04c, SPAC27E2.12, SPAPB1A10.16, SPCC1393.14, SPAC2F7.16c, SPBC16G5.19, SPBC17G9.06c, SPBC685.08, SPBC6B1.12c, SPBC800.14c, SPBP23A10.11c, SPBPB8B6.06c, SPAC15E1.03, SPBC215.15, SPAC23D3.14c, SPAC9.09, SPAPB15E9.01c, SPBC21D10.06c, SPBPB8B6.03 as kanMX4 deletions and graciously provided to us ( Spirek et al. , 2010 ). We attempted to confirm each of...”
- S. pombe genome deletion project: an update
Spirek, Cell cycle (Georgetown, Tex.) 2010 - “...SPBC365.05c * essential SPBC146.13c viable SPBC685.08 * viable SPBC16C6.09 viable SPBC6B1.12c * viable SPBC428.19c essential SPBC800.14c * viable SPCC18.04 essential SPBP23A10.11c * viable SPCC645.05c essential SPBPB8B6.03 * viable SPAC589.12 viable SPBPB8B6.06c * viable SPBC1778.01c viable SPCC290.04 * viable SPBC32F12.01c viable * genes which were missing from...”
DDB_G0274661 hypothetical protein from Dictyostelium discoideum AX4
Aligns to 55:176 / 191 (63.9%), covers 99.1% of PF08592, 57.5 bits
- The amoebal MAP kinase response to Legionella pneumophila is regulated by DupA
Li, Cell host & microbe 2009 - “...exchanger protein 0.38 0.43 1.08 Enhanced Expression DDB_G0292986 ABC transporters (3 genes) 2.252.85 2.293.17 0.731.10 DDB_G0274661 Phosphotransferase membrane protein 2.21 2.73 1.39 DDB_G0292830 sodium, hydrogen exchanger 6.67 2.16 1.00 DDB_G0283345 Sugar transporter ComD 10.69 2.89 0.77 Development Reduced Expression DDB_G0281823 V4-7,vegetative stage specific 0.34 0.09 0.26...”
hypC / A0A5N6DEZ8 noranthrone monooxygenase (EC 1.13.12.20) from Aspergillus parasiticus (see paper)
Aligns to 25:141 / 306 (38.2%), covers 68.9% of PF08592, 46.7 bits
WP_019061805 DUF1772 domain-containing protein from Streptomyces prunicolor NBRC 13075
Aligns to 45:141 / 149 (65.1%), covers 92.5% of PF08592, 44.4 bits
- Draft genome sequence of Streptomyces hyaluromycini MB-PO13T, a hyaluromycin producer
Harunari, Standards in genomic sciences 2018 - “...TP-A0875, WP_053912978 74/80 GrhO9 (71/79) RubP (74/80) 748 161 unknown hypothetical protein, Streptomyces prunicolor , WP_019061805 81/85 GrhM (80/86) RubQ (80/85) 747 174 unknown hypothetical protein, Streptomyces fulvoviolaceus , WP_030615810 67/74 GrhN (56/64) RubW (64/74) 746 623 asparagine synthase RubR, Streptomyces collinus , AAM97368 80/86 GrhP...”
CNH01920 hypothetical protein from Cryptococcus neoformans var. neoformans JEC21
Aligns to 58:161 / 172 (60.5%), covers 99.1% of PF08592, 38.2 bits
Or search for genetic data about PF08592 in the Fitness Browser
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory