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The COMPASS-mediated formation of H3K4me2/3 and the DOT1-mediated formation of H3K79me require H2BK123ub1 (By similarity)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Acetylation of histone H3 leads to transcriptional activation. H3K14ac formation by GCN5 is promoted by H3S10ph. H3K14ac can also be formed by ESA1. H3K56ac formation occurs predominantly in newly synthesized H3 molecules during G1, S and G2/M of the cell cycle and may be involved in DNA repair (By similarity)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the histone H3 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"To ensure consistency between histone entries, we follow the 'Brno' nomenclature for histone modifications, with positions referring to those used in the literature for the 'closest' model organism. Due to slight variations in histone sequences between organisms and to the presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the actual positions of modified amino acids in the sequence generally differ. In this entry the following conventions are used: H3K4me1/2/3 = mono-, di- and trimethylated Lys-5; H3K9ac = acetylated Lys-10; H3K9me1 = monomethylated Lys-10; H3S10ph = phosphorylated Ser-11; H3K14ac = acetylated Lys-15; H3K14me2 = dimethylated Lys-15; H3K18ac = acetylated Lys-19; H3K18me1 = monomethylated Lys-19; H3K23ac = acetylated Lys-24; H3K23me1 = monomethylated Lys-24; H3K27ac = acetylated Lys-28; H3K27me1/2/3 = mono-, di- and trimethylated Lys-28; H3K36ac = acetylated Lys-37; H3K36me1/2/3 = mono-, di- and trimethylated Lys-37; H3K56ac = acetylated Lys-57; H3K64ac = acetylated Lys-65; H3K79me1/2/3 = mono-, di- and trimethylated Lys-80"}],"commentType":"CAUTION"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":136,"modifier":"EXACT"}},"description":"Histone H3","featureId":"PRO_0000221363"},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Modified residue","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":5,"modifier":"EXACT"}},"description":"N6,N6,N6-trimethyllysine; 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Malpinins are acetylated hexapeptides (Ac-D-Leu/Val-D-Arg-D-Leu/Val-L-Phe/Leu-Dhb-D-Trp) containing a non-canonical amino acid derived from dehydration of L-Trp, (Z)-dehydrobutyrine (Dhb), at position 5, as well as a C-terminal D-amino acid, D-tryptophan, that can be oxidized to kynurenine (PubMed:36091214). Incorporated D-amino acids in positions 1, 3 and 4 are variable resulting in the malpinin A-congeners malpinin B to E (PubMed:36091214). Both modules M1 and M3 have relaxed specificity towards aliphatic amino acids (L-Leu > L-Met > L/D-Val > L-Cys), explaining Val at position 1 and 3 in malpinin A-congeners malpinin B to D (PubMed:36091214). The incorporation of L-Leu, but not N-acetyl-L-Leu by module 1 suggests the N-terminal acetylation occurs at a later stage of biosynthesis (PubMed:36091214). Similar to M1 and M3, M4 has a broad substrate spectrum showing the highest activity with L-Phe followed by other hydrophobic amino acids (L-Phe > L-Met = L-Trp) (PubMed:36091214). In contrast, M2, M5 and M6 are highly specific for L-Arg, L-Thr, and L-Trp, respectively (PubMed:36091214). Solely, M7 converted its preferred substrate (L-Phe) with a 15 000-fold reduced turnover rate compared to the most active module M6, indicating that its A domain cannot contribute to the malpinin biosynthesis due to low activity (PubMed:36091214). Since the last T domain in malA is apparently not loaded with an amino acid, either the TE domain must offload the oligopeptide from the preceding T domain or the dual E/C domain of M7 must transfer the final peptide chain to the free acceptor T domain of M7 prior to release (PubMed:36091214)"}],"commentType":"FUNCTION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":0.036,"unit":"mM","substrate":"L-Leu (for module 3)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36091214"}]},{"constant":0.46,"unit":"mM","substrate":"L-Val (for module 3)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36091214"}]},{"constant":4.3,"unit":"mM","substrate":"L-Met (for module 3)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36091214"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36091214"}],"value":"The kcat values of module 3 are 2.2 min(-1), 2.2 min(-1) and 2.0 min(-1) for L-Leu, L-Val and L-Met, respectively."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36091214"}],"value":"NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, epimerase (E) domains (responsible for L- to D-amino acid conversion) are present within the NRP synthetase. MalA is composed of 7 modules (M1 to M7) and contains bacterial-like dual epimerase/condensation domains allowing the racemization of enzyme-tethered L-amino acids and the subsequent incorporation of D-amino acids into the metabolites. The C domain of M6 acts as a dual dehydration/condensation domain (marked as C*). The C domain of M1 is truncated and lacks the essential C1-C4 core motifs at its N-terminal region including the highly conserved tandem His-His motif in the active site of C3. Moreover, the final adenylation domain (in M7) is inactive and offloading occurs either by the final dual E/C domain or the C-terminal T or TE domain. MalA has the following architecture: C-A-T-E/C-A-T-E/C-A-T-E/C-A-T-C-A-T-C*-A-T-E/C-A-T-TE"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30789272"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36091214"}],"value":"Mortierella alpina biosurfactants may have an enormous potential for various applications in pharmacy, health care, food, cosmetics, or textiles since they offer a highly biocompatible and biodegradable alternative for synthetic surfactants in formulations (PubMed:30789272). 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Module 3 shows promiscuous adenylation (accepting either Trp, Phe or Tyr) leading to the parallel production of multiple products from one NRPS assembly line, including malpibaldin A corresponding to cyclo(-L-Leu-D-Leu-D-Phe-L-Leu-D-Val-), malpibaldin B corresponding to cyclo(-L-Leu-D-Leu-D-Tyr-L-Leu-D-Val-) and malpibaldin C corresponding to cyclo(-Leu-Leu-Trp-Leu-Val-) (PubMed:33158886)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33158886"}],"value":"Expression is induced in the presence of fructose"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"33158886"}],"value":"NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Contains bacterial-like dual epimerase/condensation domains allowing the racemization of enzyme-tethered L-amino acids and the subsequent incorporation of D-amino acids into the metabolites. MpbA has the following architecture: C-A-T-E/C-A-T-C-A-T-E/C-A-T-E/C-A-T-TE"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30789272"}],"value":"Mortierella alpina biosurfactants may have an enormous potential for various applications in pharmacy, health care, food, cosmetics, or textiles since they offer a highly biocompatible and biodegradable alternative for synthetic surfactants in formulations"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33158886"}],"value":"The surprising structural and mechanistic similarity to bacterial nonribosomal peptide synthetases (NRPSs) points to an endobacterial origin of the Mortierella mpcA and mpbA genes that differ from their asco- and basidiomycete counterparts and may have evolved independently"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the NRP synthetase 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