Family Search for PF11807 (UstYa)

April 2024: See Interactive Tools for Functional Annotation of Bacterial Genomes for advice on using these tools.

Running HMMer for PF11807

PF11807 hits 26 sequences in PaperBLAST's database above the trusted cutoff. Showing hits to curated sequences only. Or see all hits or try another family.

APRY_ASPFN / B8NCQ4 UstYa family oxidase aprY; Asperipin-2a biosynthesis cluster protein Y; EC 1.-.-.- from Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) (see 2 papers)
Aligns to 49:278 / 334 (68.9%), covers 97.3% of PF11807, 213.1 bits

• function: UstYa family oxidase; part of the gene cluster that mediates the biosynthesis of the asperipin-2a, a bicyclic peptide that possesses two macrocyclic ether rings consisting of 14- and 17-membered paracyclophans (PubMed:26703898, PubMed:30516224). Within the pathway, aprY is responsible for the synthesis of the bicyclic structure of asperipin-2a (PubMed:30516224). The pathway starts with the processing of the precursor aprA by kexin proteases to produce 11 identical copies of the hexapeptide Phe-Tyr-Tyr-Thr-Gly-Tyr. Macrocyclization of asperipin-2a may accompany an alpha-hydroxylation-dehydration sequence to give an imine, which is readily hydrolyzed to yield putative ketone intermediate. The reductase aprR may be required for the final reduction to yield asperipin-2a (Probable).
  disruption phenotype: Abolishes the production of asperipin-2a.

PHYC1_DIALO / A0A8K1Y6E0 UstYa family oxidase phomYc; Phomopsin biosynthesis cluster protein Yc; EC 1.-.-.- from Diaporthe leptostromiformis (Lupinosis disease fungus) (Phomopsis leptostromiformis) (see paper)
Aligns to 26:249 / 256 (87.5%), covers 98.6% of PF11807, 178.0 bits

• function: UstYa family oxidase; part of the gene cluster that mediates the biosynthesis of the phomopsins, a group of hexapeptide mycotoxins which infects lupins and causes lupinosis disease in livestock (PubMed:34608734). Within the pathway, phomYc catalyzes the desaturation of the Ile moiety into 2,3-dehydroisoleucine (dIle) (PubMed:34608734). The pathway starts with the processing of the precursor phomA by several endopeptidases including kexin proteases as well as the cluster-specific S41 family peptidase phomP1 and the oligopeptidase phomG to produce 10 identical copies of the hexapeptide Tyr-Val-Ile-Pro-Ile-Asp. After being excised from the precursor peptide, the core peptides are cyclized and modified post- translationally by enzymes encoded within the gene cluster. The timing and order of proteolysis of the phomA precursor and PTMs are still unknown. Two tyrosinase-like enzymes, phomQ1 and phomQ2, catalyze the chlorination and hydroxylation of Tyr, respectively. PhomYb, is proposed to be involved in the construction of the macrocyclic structure. The other 4 ustYa family proteins may be involved in PTMs that generate the unique structure of phomopsin A. PhomYa is required for the hydroxylation of C-beta of Tyr. PhomYc, phomYd, and phomYe are responsible for the biosynthesis of 2,3-dehydroisoleucine (dIle), 2,3- dehydroaspartic acid (dAsp), and 3,4-dehydroproline (dPro), respectively. While dIle formation by phomYc is indispensable for the installation of dAsp by phomYd, the order of the other PTMs have not been elucidated yet. Most of the biosynthetic enzymes likely have broad substrate specificity, and thus, there might be a metabolic grid from a precursor to phomopsin A. The enzyme(s) responsible for the biosynthesis of 3,4-dehydrovaline (dVal) have also not been identified yet. Finally, phomM acts as an S-adenosylmethionine-dependent alpha-N- methyltransferase that catalyzes two successive N-methylation reactions, converting N-desmethyl-phomopsin A to phomopsin A and phomopsin A further to an N,N-dimethylated congener called phomopsin E (Probable).
  disruption phenotype: Abolishes the formation of phomopsin A and leads to the accumulation an intermediate with no modified Ile moiety.

PHYC2_DIALO / A0A142I736 UstYa family oxidase phomYc'; Phomopsin biosynthesis cluster protein Yc'a; EC 1.-.-.- from Diaporthe leptostromiformis (Lupinosis disease fungus) (Phomopsis leptostromiformis) (see paper)
Aligns to 26:229 / 254 (80.3%), covers 98.6% of PF11807, 156.9 bits

• function: UstYa family oxidase; part of the gene cluster that mediates the biosynthesis of the phomopsins, a group of hexapeptide mycotoxins which infects lupins and causes lupinosis disease in livestock (PubMed:34608734). Within the pathway, phomYc' catalyzes the desaturation of the Ile moiety into 2,3-dehydroisoleucine (dIle) (PubMed:34608734). The pathway starts with the processing of the precursor phomA' by several endopeptidases including kexin proteases as well as the cluster-specific S41 family peptidase phomP1 and the oligopeptidase phomG' to produce 10 identical copies of the hexapeptide Tyr-Val-Ile-Pro-Ile-Asp. After being excised from the precursor peptide, the core peptides are cyclized and modified post- translationally by enzymes encoded within the gene cluster. The timing and order of proteolysis of the phomA' precursor and PTMs are still unknown. Two tyrosinase-like enzymes, phomQ1' and phomQ2, catalyze the chlorination and hydroxylation of Tyr, respectively. PhomYb, is proposed to be involved in the construction of the macrocyclic structure. The other 4 ustYa family proteins may be involved in PTMs that generate the unique structure of phomopsin A. PhomYa' is required for the hydroxylation of C-beta of Tyr. PhomYc', phomYd', and phomYe are responsible for the biosynthesis of 2,3-dehydroisoleucine (dIle), 2,3-dehydroaspartic acid (dAsp), and 3,4-dehydroproline (dPro), respectively. While dIle formation by phomYc' is indispensable for the installation of dAsp by phomYd', the order of the other PTMs have not been elucidated yet. Most of the biosynthetic enzymes likely have broad substrate specificity, and thus, there might be a metabolic grid from a precursor to phomopsin A. The enzyme(s) responsible for the biosynthesis of 3,4-dehydrovaline (dVal) have also not been identified yet. Finally, phomM' acts as an S-adenosylmethionine-dependent alpha-N- methyltransferase that catalyzes two successive N-methylation reactions, converting N-desmethyl-phomopsin A to phomopsin A and phomopsin A further to an N,N-dimethylated congener called phomopsin E (Probable).

CCTO_TALIS / A0A0U1LQF6 Transacylase cctO; Cyclochlorotine biosynthesis protein O; EC 2.3.1.- from Talaromyces islandicus (Penicillium islandicum) (see 2 papers)
Aligns to 37:281 / 300 (81.7%), covers 93.2% of PF11807, 122.3 bits

• function: Transacylase; part of the gene cluster that mediates the biosynthesis of the mycotoxin cyclochlorotine, a hepatotoxic and carcinogenic cyclic chlorinated pentapeptide (PubMed:26954535, PubMed:33736433). Within the pathway, cctO catalyzes the intramolecular O,N-transacylation from isocyclochlorotine to cyclochlorotine (PubMed:33736433). The NRPS cctN initially catalyzes the condensation of L-serine (Ser), Pro, L-2-aminobutyrate (2Abu), Ser, and beta-Phe in this order to produce isocyclotine. After the dichlorination of Pro2 catalyzed by cctP2 to produce isocyclochlorotine, the cctO-mediated transacylation of isocyclochlorotine can furnish cyclochlorotine. The subsequent hydroxylation of cyclochlorotine by cctR yields hydroxycyclochlorotine as the final product. CctP1 probably acts as a phenylalanine aminomutase and provides the uncommon building block beta-Phe. Furthermore, 2Abu can be synthesized from threonine by one of the threonine dehydratases and transaminases localized outside of the cluster. The functions of the remaining proteins encoded by the cluster, cctM and cctT, have not been identified yet (PubMed:33736433) (Probable).
  disruption phenotype: Leads to the accumulation of isocyclochlorotine.

PHYD1_DIALO / A0A8J9R8Y7 UstYa family oxidase phomYd; Phomopsin biosynthesis cluster protein Yd; EC 1.-.-.- from Diaporthe leptostromiformis (Lupinosis disease fungus) (Phomopsis leptostromiformis) (see paper)
Aligns to 38:273 / 301 (78.4%), covers 98.6% of PF11807, 107.3 bits

• function: UstYa family oxidase; part of the gene cluster that mediates the biosynthesis of the phomopsins, a group of hexapeptide mycotoxins which infects lupins and causes lupinosis disease in livestock (PubMed:34608734). Within the pathway, phomYd catalyzes the desaturation of the Asp moiety into 2,3-dehydroaspartic acid (dAsp) (PubMed:34608734). The pathway starts with the processing of the precursor phomA by several endopeptidases including kexin proteases as well as the cluster-specific S41 family peptidase phomP1 and the oligopeptidase phomG to produce 10 identical copies of the hexapeptide Tyr-Val-Ile-Pro-Ile-Asp. After being excised from the precursor peptide, the core peptides are cyclized and modified post- translationally by enzymes encoded within the gene cluster. The timing and order of proteolysis of the phomA precursor and PTMs are still unknown. Two tyrosinase-like enzymes, phomQ1 and phomQ2, catalyze the chlorination and hydroxylation of Tyr, respectively. PhomYb, is proposed to be involved in the construction of the macrocyclic structure. The other 4 ustYa family proteins may be involved in PTMs that generate the unique structure of phomopsin A. PhomYa is required for the hydroxylation of C-beta of Tyr. PhomYc, phomYd, and phomYe are responsible for the biosynthesis of 2,3-dehydroisoleucine (dIle), 2,3- dehydroaspartic acid (dAsp), and 3,4-dehydroproline (dPro), respectively. While dIle formation by phomYc is indispensable for the installation of dAsp by phomYd, the order of the other PTMs have not been elucidated yet. Most of the biosynthetic enzymes likely have broad substrate specificity, and thus, there might be a metabolic grid from a precursor to phomopsin A. The enzyme(s) responsible for the biosynthesis of 3,4-dehydrovaline (dVal) have also not been identified yet. Finally, phomM acts as an S-adenosylmethionine-dependent alpha-N- methyltransferase that catalyzes two successive N-methylation reactions, converting N-desmethyl-phomopsin A to phomopsin A and phomopsin A further to an N,N-dimethylated congener called phomopsin E (Probable).
  disruption phenotype: Abolishes the formation of phomopsin A and leads to the accumulation an intermediate with no modified Asp moiety.

PHOYB_DIALO / A0A142I729 UstYa family oxidase phomYb; Phomopsin biosynthesis cluster protein Yb; EC 1.-.-.- from Diaporthe leptostromiformis (Lupinosis disease fungus) (Phomopsis leptostromiformis) (see 2 papers)
Aligns to 44:241 / 251 (78.9%), covers 96.8% of PF11807, 98.7 bits

• function: UstYa family oxidase; part of the gene cluster that mediates the biosynthesis of the phomopsins, a group of hexapeptide mycotoxins which infects lupins and causes lupinosis disease in livestock (PubMed:26979951, PubMed:34608734). Within the pathway, phomYb is probably involved in the construction of the macrocyclic structure of the phomopsins (PubMed:34608734). The pathway starts with the processing of the precursor phomA by several endopeptidases including kexin proteases as well as the cluster-specific S41 family peptidase phomP1 and the oligopeptidase phomG to produce 10 identical copies of the hexapeptide Tyr-Val-Ile-Pro-Ile-Asp. After being excised from the precursor peptide, the core peptides are cyclized and modified post- translationally by enzymes encoded within the gene cluster. The timing and order of proteolysis of the phomA precursor and PTMs are still unknown. Two tyrosinase-like enzymes, phomQ1 and phomQ2, catalyze the chlorination and hydroxylation of Tyr, respectively. PhomYb, is proposed to be involved in the construction of the macrocyclic structure. The other 4 ustYa family proteins may be involved in PTMs that generate the unique structure of phomopsin A. PhomYa is required for the hydroxylation of C-beta of Tyr. PhomYc, phomYd, and phomYe are responsible for the biosynthesis of 2,3-dehydroisoleucine (dIle), 2,3- dehydroaspartic acid (dAsp), and 3,4-dehydroproline (dPro), respectively. While dIle formation by phomYc is indispensable for the installation of dAsp by phomYd, the order of the other PTMs have not been elucidated yet. Most of the biosynthetic enzymes likely have broad substrate specificity, and thus, there might be a metabolic grid from a precursor to phomopsin A. The enzyme(s) responsible for the biosynthesis of 3,4-dehydrovaline (dVal) have also not been identified yet. Finally, phomM acts as an S-adenosylmethionine-dependent alpha-N- methyltransferase that catalyzes two successive N-methylation reactions, converting N-desmethyl-phomopsin A to phomopsin A and phomopsin A further to an N,N-dimethylated congener called phomopsin E (Probable).
  disruption phenotype: Abolishes the formation of phomopsin A and related metabolites.

USTYA_ASPFN / B8NM67 Oxidase ustYa; Ustiloxin B biosynthesis protein Ya; EC 1.-.-.- from Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) (see 3 papers)
Aligns to 83:204 / 213 (57.3%), covers 52.7% of PF11807, 95.1 bits

• function: Oxidase; part of the gene cluster that mediates the biosynthesis of the secondary metabolite ustiloxin B, an antimitotic tetrapeptide (PubMed:24841822, PubMed:27166860, PubMed:26703898). First, ustA is processed by the subtilisin-like endoprotease Kex2 that is outside the ustiloxin B gene cluster, at the C-terminal side of Arg- Lys, after transfer to Golgi apparatus through the endoplasmic reticulum (ER) (PubMed:24841822). Cleavage by KEX2 generates 16 peptides YAIG-I to YAIG-XVI (PubMed:24841822). To process the precursor peptide further, at least two peptidases are necessary to cleave the N- terminal and C-terminal sides of the Tyr-Ala-Ile-Gly core peptide which serves as backbone for the synthesis of ustiloxin B, through cyclization and modification of the tyrosine with a non-protein coding amino acid, norvaline (PubMed:24841822). One of the two peptidases must be the serine peptidase ustP; and the other pepdidase is probably ustH (PubMed:24841822). Macrocyclization of the core peptide derived from ustA requires the tyrosinase ustQ, as well as the homologous oxidases ustYa and ustYb, and leads to the production of the first cyclization product N-desmethylustiloxin F (PubMed:27166860, PubMed:26703898). For the formation of N-desmethylustiloxin F, three oxidation steps are required, hydroxylation at the benzylic position, hydroxylation at either the aromatic ring of Tyr or beta-position of Ile, and oxidative cyclization (PubMed:27166860). UstQ may catalyze the oxidation of a phenol moiety, whereas the ustYa and ustYb are most likely responsible for the remaining two-step oxidations (PubMed:27166860). N- desmethylustiloxin F is then methylated by ustM to yield ustiloxin F which in turn substrate of the cytochrome P450 monooxygenase ustC which catalyzes the formation of S-deoxyustiloxin H (PubMed:27166860). The flavoprotein monooxygenases ustF1 and ustF2 then participate in the modification of the side chain of S-deoxyustiloxin H, leading to the synthesis of an oxime intermediate, via ustiloxin H (PubMed:27166860). Finally, carboxylative dehydration performed by the cysteine desulfurase-like protein ustD yields ustiloxin B (PubMed:27166860).
  disruption phenotype: Decreases the production of ustiloxin B (PubMed:24841822, PubMed:26703898).

CCTR_TALIS / A0A0U1LR74 Hydroxylase cctR; Cyclochlorotine biosynthesis protein R; EC 1.-.-.- from Talaromyces islandicus (Penicillium islandicum) (see 2 papers)
Aligns to 26:226 / 261 (77.0%), covers 98.2% of PF11807, 93.6 bits

• function: Hydroxylase; part of the gene cluster that mediates the biosynthesis of the mycotoxin cyclochlorotine, a hepatotoxic and carcinogenic cyclic chlorinated pentapeptide (PubMed:26954535, PubMed:33736433). Within the pathway, cctR performs the last step by hydroxylating cyclochlorotine to yield hydroxycyclochlorotine (PubMed:33736433). The NRPS cctN initially catalyzes the condensation of L-serine (Ser), Pro, L-2-aminobutyrate (2Abu), Ser, and beta-Phe in this order to produce isocyclotine. After the dichlorination of Pro2 catalyzed by cctP2 to produce isocyclochlorotine, the cctO-mediated transacylation of isocyclochlorotine can furnish cyclochlorotine. The subsequent hydroxylation of cyclochlorotine by cctR yields hydroxycyclochlorotine as the final product. CctP1 probably acts as a phenylalanine aminomutase and provides the uncommon building block beta-Phe. Furthermore, 2Abu can be synthesized from threonine by one of the threonine dehydratases and transaminases localized outside of the cluster. The functions of the remaining proteins encoded by the cluster, cctM and cctT, have not been identified yet (PubMed:33736433) (Probable).
  disruption phenotype: Abolishes the production of hydroxycyclochlorotine.

PHOYE_DIALO / A0A142I739 UstYa family oxidase phomYe; Phomopsin biosynthesis cluster protein Ye; EC 1.-.-.- from Diaporthe leptostromiformis (Lupinosis disease fungus) (Phomopsis leptostromiformis) (see paper)
Aligns to 24:264 / 285 (84.6%), covers 49.1% of PF11807, 87.3 bits

• function: UstYa family oxidase; part of the gene cluster that mediates the biosynthesis of the phomopsins, a group of hexapeptide mycotoxins which infects lupins and causes lupinosis disease in livestock (PubMed:34608734). Within the pathway, phomYe catalyzes the desaturation of the Pro moiety into 3,4-dehydroproline (dPro) (PubMed:34608734). The pathway starts with the processing of the precursor phomA by several endopeptidases including kexin proteases as well as the cluster-specific S41 family peptidase phomP1 and the oligopeptidase phomG to produce 10 identical copies of the hexapeptide Tyr-Val-Ile-Pro-Ile-Asp. After being excised from the precursor peptide, the core peptides are cyclized and modified post- translationally by enzymes encoded within the gene cluster. The timing and order of proteolysis of the phomA precursor and PTMs are still unknown. Two tyrosinase-like enzymes, phomQ1 and phomQ2, catalyze the chlorination and hydroxylation of Tyr, respectively. PhomYb, is proposed to be involved in the construction of the macrocyclic structure. The other 4 ustYa family proteins may be involved in PTMs that generate the unique structure of phomopsin A. PhomYa is required for the hydroxylation of C-beta of Tyr. PhomYc, phomYd, and phomYe are responsible for the biosynthesis of 2,3-dehydroisoleucine (dIle), 2,3- dehydroaspartic acid (dAsp), and 3,4-dehydroproline (dPro), respectively. While dIle formation by phomYc is indispensable for the installation of dAsp by phomYd, the order of the other PTMs have not been elucidated yet. Most of the biosynthetic enzymes likely have broad substrate specificity, and thus, there might be a metabolic grid from a precursor to phomopsin A. The enzyme(s) responsible for the biosynthesis of 3,4-dehydrovaline (dVal) have also not been identified yet. Finally, phomM acts as an S-adenosylmethionine-dependent alpha-N- methyltransferase that catalyzes two successive N-methylation reactions, converting N-desmethyl-phomopsin A to phomopsin A and phomopsin A further to an N,N-dimethylated congener called phomopsin E (Probable).
  disruption phenotype: Abolishes the formation of phomopsin A and leads to the accumulation an intermediate with no modified Pro moiety.

USTYB_ASPFN / B8NM70 Oxidase ustYb; Ustiloxin B biosynthesis protein Yb; EC 1.-.-.- from Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) (see 3 papers)
Aligns to 21:251 / 259 (89.2%), covers 94.5% of PF11807, 84.1 bits

• function: Oxidase; part of the gene cluster that mediates the biosynthesis of the secondary metabolite ustiloxin B, an antimitotic tetrapeptide (PubMed:24841822, PubMed:27166860, PubMed:26703898). First, ustA is processed by the subtilisin-like endoprotease Kex2 that is outside the ustiloxin B gene cluster, at the C-terminal side of Arg- Lys, after transfer to Golgi apparatus through the endoplasmic reticulum (ER) (PubMed:24841822). Cleavage by KEX2 generates 16 peptides YAIG-I to YAIG-XVI (PubMed:24841822). To process the precursor peptide further, at least two peptidases are necessary to cleave the N- terminal and C-terminal sides of the Tyr-Ala-Ile-Gly core peptide which serves as backbone for the synthesis of ustiloxin B, through cyclization and modification of the tyrosine with a non-protein coding amino acid, norvaline (PubMed:24841822). One of the two peptidases must be the serine peptidase ustP; and the other pepdidase is probably ustH (PubMed:24841822). Macrocyclization of the core peptide derived from ustA requires the tyrosinase ustQ, as well as the homologous oxidases ustYa and ustYb, and leads to the production of the first cyclization product N-desmethylustiloxin F (PubMed:27166860, PubMed:26703898). For the formation of N-desmethylustiloxin F, three oxidation steps are required, hydroxylation at the benzylic position, hydroxylation at either the aromatic ring of Tyr or beta-position of Ile, and oxidative cyclization (PubMed:27166860). UstQ may catalyze the oxidation of a phenol moiety, whereas the ustYa and ustYb are most likely responsible for the remaining two-step oxidations (PubMed:27166860). N- desmethylustiloxin F is then methylated by ustM to yield ustiloxin F which in turn substrate of the cytochrome P450 monooxygenase ustC which catalyzes the formation of S-deoxyustiloxin H (PubMed:27166860). The flavoprotein monooxygenases ustF1 and ustF2 then participate in the modification of the side chain of S-deoxyustiloxin H, leading to the synthesis of an oxime intermediate, via ustiloxin H (PubMed:27166860). Finally, carboxylative dehydration performed by the cysteine desulfurase-like protein ustD yields ustiloxin B (PubMed:27166860).
  disruption phenotype: Decreases the production of ustiloxin B (PubMed:24841822, PubMed:26703898).

PHOYA_DIALO / A0A8J9WH54 UstYa family oxidase phomYa; Phomopsin biosynthesis cluster protein Ya; EC 1.-.-.- from Diaporthe leptostromiformis (Lupinosis disease fungus) (Phomopsis leptostromiformis) (see paper)
Aligns to 30:257 / 262 (87.0%), covers 69.5% of PF11807, 83.8 bits

• function: UstYa family oxidase; part of the gene cluster that mediates the biosynthesis of the phomopsins, a group of hexapeptide mycotoxins which infects lupins and causes lupinosis disease in livestock (PubMed:34608734). Within the pathway, phomYa catalyzes the hydroxylation of C-beta of Tyr (PubMed:34608734). The pathway starts with the processing of the precursor phomA by several endopeptidases including kexin proteases as well as the cluster-specific S41 family peptidase phomP1 and the oligopeptidase phomG to produce 10 identical copies of the hexapeptide Tyr-Val-Ile-Pro-Ile-Asp. After being excised from the precursor peptide, the core peptides are cyclized and modified post-translationally by enzymes encoded within the gene cluster. The timing and order of proteolysis of the phomA precursor and PTMs are still unknown. Two tyrosinase-like enzymes, phomQ1 and phomQ2, catalyze the chlorination and hydroxylation of Tyr, respectively. PhomYb, is proposed to be involved in the construction of the macrocyclic structure. The other 4 ustYa family proteins may be involved in PTMs that generate the unique structure of phomopsin A. PhomYa is required for the hydroxylation of C-beta of Tyr. PhomYc, phomYd, and phomYe are responsible for the biosynthesis of 2,3-dehydroisoleucine (dIle), 2,3- dehydroaspartic acid (dAsp), and 3,4-dehydroproline (dPro), respectively. While dIle formation by phomYc is indispensable for the installation of dAsp by phomYd, the order of the other PTMs have not been elucidated yet. Most of the biosynthetic enzymes likely have broad substrate specificity, and thus, there might be a metabolic grid from a precursor to phomopsin A. The enzyme(s) responsible for the biosynthesis of 3,4-dehydrovaline (dVal) have also not been identified yet. Finally, phomM acts as an S-adenosylmethionine-dependent alpha-N- methyltransferase that catalyzes two successive N-methylation reactions, converting N-desmethyl-phomopsin A to phomopsin A and phomopsin A further to an N,N-dimethylated congener called phomopsin E (Probable).
  disruption phenotype: Abolishes the formation of phomopsin A and leads to the accumulation of a deoxy derivative of phomopsin A.

VICYB_BIPV3 / W7E0Q5 UstYa family oxidase VicYb; Victorin biosynthesis cluster protein Yb; EC 1.-.-.- from Bipolaris victoriae (strain FI3) (Victoria blight of oats agent) (Cochliobolus victoriae) (see paper)
Aligns to 1:91 / 112 (81.2%), covers 43.2% of PF11807, 76.6 bits

• function: UstYa family oxidase, part of the gene cluster that mediates the biosynthesis of the secondary metabolite victorin, the molecular basis for Victoria blight of oats (PubMed:32929037). Within the pathway, vicYb catalyzes the oxidative cyclization of the core peptide (PubMed:32929037). The pathway starts with the processing of the precursor vicA1 by several endopeptidases including kexin proteases as well as the cluster-specific S28 family peptidases vicPa and vicPb to produce 7 identical copies of the hexapeptide Gly-Leu-Lys-Leu-Ala-Phe. After being excised from the precursor peptide, the core peptides are cyclized and modified post-translationally by enzymes encoded within the gene cluster. The ustYa family oxidase vicYb is required for the formation of the macrocycle in victorin and the copper amine oxidases (CAOs) vicK1 and vicK2 are responsible for converting victorin to the active form by oxidizing the N-terminal glycyl residue in the peptides to glyoxylate. Relaxed substrate specificity of enzymes in the victorin biosynthetic pathway results in a metabolic grid that produces a set of analogs including victorinines B, C, E or HV-toxin M (Probable).
  disruption phenotype: Impairs the production of victorin or of any victorin derivative or intermediate.

CCTP2_TALIS / P9WEN7 Chlorinase cctP2; Cyclochlorotine biosynthesis protein P2; EC 2.5.1.- from Talaromyces islandicus (Penicillium islandicum) (see paper)
Aligns to 31:230 / 314 (63.7%), covers 97.3% of PF11807, 74.9 bits

• function: Chlorinase; part of the gene cluster that mediates the biosynthesis of the mycotoxin cyclochlorotine, a hepatotoxic and carcinogenic cyclic chlorinated pentapeptide (PubMed:33736433). Within the pathway, cctP2 catalyzes the formation of isocyclochlorotine via dichlorination of the Pro from the isocyclotine skeleton (PubMed:33736433). The NRPS cctN initially catalyzes the condensation of L-serine (Ser), Pro, L-2-aminobutyrate (2Abu), Ser, and beta-Phe in this order to produce isocyclotine. After the dichlorination of Pro2 catalyzed by cctP2 to produce isocyclochlorotine, the cctO-mediated transacylation of isocyclochlorotine can furnish cyclochlorotine. The subsequent hydroxylation of cyclochlorotine by cctR yields hydroxycyclochlorotine as the final product. CctP1 probably acts as a phenylalanine aminomutase and provides the uncommon building block beta-Phe. Furthermore, 2Abu can be synthesized from threonine by one of the threonine dehydratases and transaminases localized outside of the cluster. The functions of the remaining proteins encoded by the cluster, cctM and cctT, have not been identified yet (PubMed:33736433) (Probable).
  disruption phenotype: Abolishes the production of chlorinated derivatives cyclochlorotine and hydroxycyclochlorotine and leads to the accumulatin of isocyclotine.

VICYC_BIPV3 / W7DZP2 UstYa family oxidase VicYc; Victorin biosynthesis cluster protein Yc; EC 1.-.-.- from Bipolaris victoriae (strain FI3) (Victoria blight of oats agent) (Cochliobolus victoriae) (see paper)
Aligns to 3:91 / 97 (91.8%), covers 41.8% of PF11807, 71.8 bits

• function: UstYa family oxidase, part of the gene cluster that mediates the biosynthesis of the secondary metabolite victorin, the molecular basis for Victoria blight of oats (PubMed:32929037). The role of vicYc within the pathway has still to be determined (PubMed:32929037). The pathway starts with the processing of the precursor vicA1 by several endopeptidases including kexin proteases as well as the cluster- specific S28 family peptidases vicPa and vicPb to produce 7 identical copies of the hexapeptide Gly-Leu-Lys-Leu-Ala-Phe. After being excised from the precursor peptide, the core peptides are cyclized and modified post-translationally by enzymes encoded within the gene cluster. The ustYa family oxidase vicYb is required for the formation of the macrocycle in victorin and the copper amine oxidases (CAOs) vicK1 and vicK2 are responsible for converting victorin to the active form by oxidizing the N-terminal glycyl residue in the peptides to glyoxylate. Relaxed substrate specificity of enzymes in the victorin biosynthetic pathway results in a metabolic grid that produces a set of analogs including victorinines B, C, E or HV-toxin M (Probable).

PHYD2_DIALO / A0A142I738 UstYa family oxidase phomYd'; Phomopsin biosynthesis cluster protein Yd'; EC 1.-.-.- from Diaporthe leptostromiformis (Lupinosis disease fungus) (Phomopsis leptostromiformis) (see paper)
Aligns to 148:206 / 234 (25.2%), covers 25.9% of PF11807, 55.3 bits

• function: UstYa family oxidase; part of the gene cluster that mediates the biosynthesis of the phomopsins, a group of hexapeptide mycotoxins which infects lupins and causes lupinosis disease in livestock (PubMed:34608734). Within the pathway, phomYd' catalyzes the desaturation of the Asp moiety into 2,3-dehydroaspartic acid (dAsp) (PubMed:34608734). The pathway starts with the processing of the precursor phomA' by several endopeptidases including kexin proteases as well as the cluster-specific S41 family peptidase phomP1 and the oligopeptidase phomG' to produce 10 identical copies of the hexapeptide Tyr-Val-Ile-Pro-Ile-Asp. After being excised from the precursor peptide, the core peptides are cyclized and modified post- translationally by enzymes encoded within the gene cluster. The timing and order of proteolysis of the phomA' precursor and PTMs are still unknown. Two tyrosinase-like enzymes, phomQ1' and phomQ2, catalyze the chlorination and hydroxylation of Tyr, respectively. PhomYb, is proposed to be involved in the construction of the macrocyclic structure. The other 4 ustYa family proteins may be involved in PTMs that generate the unique structure of phomopsin A. PhomYa' is required for the hydroxylation of C-beta of Tyr. PhomYc', phomYd', and phomYe are responsible for the biosynthesis of 2,3-dehydroisoleucine (dIle), 2,3-dehydroaspartic acid (dAsp), and 3,4-dehydroproline (dPro), respectively. While dIle formation by phomYc' is indispensable for the installation of dAsp by phomYd', the order of the other PTMs have not been elucidated yet. Most of the biosynthetic enzymes likely have broad substrate specificity, and thus, there might be a metabolic grid from a precursor to phomopsin A. The enzyme(s) responsible for the biosynthesis of 3,4-dehydrovaline (dVal) have also not been identified yet. Finally, phomM' acts as an S-adenosylmethionine-dependent alpha-N- methyltransferase that catalyzes two successive N-methylation reactions, converting N-desmethyl-phomopsin A to phomopsin A and phomopsin A further to an N,N-dimethylated congener called phomopsin E (Probable).

VICYA_BIPV3 / W7E4C5 UstYa family oxidase VicYa; Victorin biosynthesis cluster protein Ya; EC 1.-.-.- from Bipolaris victoriae (strain FI3) (Victoria blight of oats agent) (Cochliobolus victoriae) (see paper)
Aligns to 19:148 / 159 (81.8%), covers 44.5% of PF11807, 55.2 bits

• function: UstYa family oxidase, part of the gene cluster that mediates the biosynthesis of the secondary metabolite victorin, the molecular basis for Victoria blight of oats (PubMed:32929037). The role of vicYa within the pathway has still to be determined (PubMed:32929037). The pathway starts with the processing of the precursor vicA1 by several endopeptidases including kexin proteases as well as the cluster- specific S28 family peptidases vicPa and vicPb to produce 7 identical copies of the hexapeptide Gly-Leu-Lys-Leu-Ala-Phe. After being excised from the precursor peptide, the core peptides are cyclized and modified post-translationally by enzymes encoded within the gene cluster. The ustYa family oxidase vicYb is required for the formation of the macrocycle in victorin and the copper amine oxidases (CAOs) vicK1 and vicK2 are responsible for converting victorin to the active form by oxidizing the N-terminal glycyl residue in the peptides to glyoxylate. Relaxed substrate specificity of enzymes in the victorin biosynthetic pathway results in a metabolic grid that produces a set of analogs including victorinines B, C, E or HV-toxin M (Probable).

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