About Products Protein Database Contact

lnaB

Gene
lnaB
Protein
NmrA-like family domain-containing oxidoreductase lnbB
Organism
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
Length
335 amino acids
Function
NmrA-like family domain-containing oxidoreductase; part of the lnb gene cluster that mediates the biosynthesis of diastereomeric piperazines. Lna and lnb clusters encode sets of enzymes that produce overlapping sets of previously undescribed metabolites such as piperazinomycin-like metabolites or morpholine (PubMed:23281040). The lna and lnb biosynthetic pathways appear to be part of a signaling network that controls the formation of sclerotia, a resilient overwintering structure (PubMed:23281040). One primary function of the non-canonical nonribosomal peptide synthetases lnaA and lnbA consists in the reduction of L-tyrosine (PubMed:23281040). The presence in the clusters of tailoring enzymes such as the oxidoreductases lnaB, lnbB, lnaE or lnbE, as well as of the cytochrome P450 monooxygenases lnaC, lnaD, or lnbC, might explain formation of various diastereomeric piperazines (PubMed:23281040).
Similarity
Belongs to the NmrA-type oxidoreductase family.
Mass
37.067 kDa
Sequence
MTVTATERIVTVFGTGNQAGAVARALLADKTSQFKVRAISRHPDSASSRTLSALGVQVVKADGWNLEELTRAFADTWAAFVNTNSDDPLFLQKGDGPTEFDLGKNIIDSLVAAKVQHLVYSCFASSVEQTKGKLFIKPMEMKYQALKYARETGHFATTCGIYAAWYYEQFLDKATADVFGGFPTTPDEEGYITFRAPLWGDDEHPSFVSITHDFGDMVHGILLEPEQWDGKSVPAASDVMTFEQLAQTLQNATGRKSRYIPLPSWEDFGRGIPELDDHKLLFAFTQATGGRYFGDVPTETKTALRLKRRAAEAQGKSGNEANLLSMEEWFKTNFA

Gene
lnaB
Protein
NmrA-like family domain-containing oxidoreductase lnbB
Organism
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
Length
335 amino acids
Function
NmrA-like family domain-containing oxidoreductase; part of the lnb gene cluster that mediates the biosynthesis of diastereomeric piperazines. Lna and lnb clusters encode sets of enzymes that produce overlapping sets of previously undescribed metabolites such as piperazinomycin-like metabolites or morpholine (PubMed:23281040). The lna and lnb biosynthetic pathways appear to be part of a signaling network that controls the formation of sclerotia, a resilient overwintering structure (PubMed:23281040). One primary function of the non-canonical nonribosomal peptide synthetases lnaA and lnbA consists in the reduction of L-tyrosine (PubMed:23281040). The presence in the clusters of tailoring enzymes such as the oxidoreductases lnaB, lnbB, lnaE or lnbE, as well as of the cytochrome P450 monooxygenases lnaC, lnaD, or lnbC, might explain formation of various diastereomeric piperazines (PubMed:23281040).
Similarity
Belongs to the NmrA-type oxidoreductase family.
Mass
37.067 kDa
Sequence
MTVTATERIVTVFGTGNQAGAVARALLADKTSQFKVRAISRHPDSASSRTLSALGVQVVKADGWNLEELTRAFADTWAAFVNTNSDDPLFLQKGDGPTEFDLGKNIIDSLVAAKVQHLVYSCFASSVEQTKGKLFIKPMEMKYQALKYARETGHFATTCGIYAAWYYEQFLDKATADVFGGFPTTPDEEGYITFRAPLWGDDEHPSFVSITHDFGDMVHGILLEPEQWDGKSVPAASDVMTFEQLAQTLQNATGRKSRYIPLPSWEDFGRGIPELDDHKLLFAFTQATGGRYFGDVPTETKTALRLKRRAAEAQGKSGNEANLLSMEEWFKTNFA

Gene
lnaB
Protein
NmrA-like family domain-containing oxidoreductase lnaB
Organism
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
Length
334 amino acids
Function
NmrA-like family domain-containing oxidoreductase; part of the lna gene cluster that mediates the biosynthesis of diastereomeric piperazines. Lna and lnb clusters encode sets of enzymes that produce overlapping sets of previously undescribed metabolites such as piperazinomycin-like metabolites or morpholine (PubMed:23281040). The lna and lnb biosynthetic pathways appear to be part of a signaling network that controls the formation of sclerotia, a resilient overwintering structure (PubMed:23281040). One primary function of the non-canonical nonribosomal peptide synthetases lnaA and lnbA consists in the reduction of L-tyrosine (PubMed:23281040). The presence in the clusters of tailoring enzymes such as the oxidoreductases lnaB, lnbB, lnaE or lnbE, as well as of the cytochrome P450 monooxygenases lnaC, lnaD, or lnbC, might explain formation of various diastereomeric piperazines (PubMed:23281040).
Similarity
Belongs to the NmrA-type oxidoreductase family.
Mass
36.713 kDa
Sequence
MSPDRKLITIFGGTGKQGGSVAHSLLQNPDFRVRVITRNAQSDASRKLAALGADIAQGDGFSGDEMLSAFSGSWGAFVNINSDDKIFTTEGGPTEFDMGKIIVDSAVQAGVKHLVFSSGPPCTEMTNGRVRMKAMDMKNKIEQYARSLGSFETFTPIGAGWFLENFLGKEVAPVFGGFPYFPDDQGYLTFRVPYWGGDEHVPWLSISDDFGDIVQGIFLDPGRWNGHFVHGVSDIRSFEQVVADFAAVTGNKARFQPILPTWEAFDTHGIQELEDVKLMFGFTQLTGGRYFGPEDTEVDTARQLKQITGLKLGRPEGQHKLTSARDWFAARFAN

Gene
lnaB
Protein
NmrA-like family domain-containing oxidoreductase lnaB
Organism
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
Length
334 amino acids
Function
NmrA-like family domain-containing oxidoreductase; part of the lna gene cluster that mediates the biosynthesis of diastereomeric piperazines. Lna and lnb clusters encode sets of enzymes that produce overlapping sets of previously undescribed metabolites such as piperazinomycin-like metabolites or morpholine (PubMed:23281040). The lna and lnb biosynthetic pathways appear to be part of a signaling network that controls the formation of sclerotia, a resilient overwintering structure (PubMed:23281040). One primary function of the non-canonical nonribosomal peptide synthetases lnaA and lnbA consists in the reduction of L-tyrosine (PubMed:23281040). The presence in the clusters of tailoring enzymes such as the oxidoreductases lnaB, lnbB, lnaE or lnbE, as well as of the cytochrome P450 monooxygenases lnaC, lnaD, or lnbC, might explain formation of various diastereomeric piperazines (PubMed:23281040).
Similarity
Belongs to the NmrA-type oxidoreductase family.
Mass
36.713 kDa
Sequence
MSPDRKLITIFGGTGKQGGSVAHSLLQNPDFRVRVITRNAQSDASRKLAALGADIAQGDGFSGDEMLSAFSGSWGAFVNINSDDKIFTTEGGPTEFDMGKIIVDSAVQAGVKHLVFSSGPPCTEMTNGRVRMKAMDMKNKIEQYARSLGSFETFTPIGAGWFLENFLGKEVAPVFGGFPYFPDDQGYLTFRVPYWGGDEHVPWLSISDDFGDIVQGIFLDPGRWNGHFVHGVSDIRSFEQVVADFAAVTGNKARFQPILPTWEAFDTHGIQELEDVKLMFGFTQLTGGRYFGPEDTEVDTARQLKQITGLKLGRPEGQHKLTSARDWFAARFAN