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Information on EC 2.4.1.338 - validoxylamine A glucosyltransferase
for references in articles please use BRENDA:EC2.4.1.338
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.338 validoxylamine A glucosyltransferase
IUBMB Comments
The enzyme, characterized from the bacterium Streptomyces hygroscopicus subsp. limoneus, catalyses the ultimate step in the biosynthesis of the antifungal agent validamycin A.
The expected taxonomic range for this enzyme is: Streptomyces hygroscopicus
showSynonyms
valG, vldE, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
valG
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-glucose + validoxylamine A = UDP + validamycin A
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
validamycin biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
UDP-alpha-D-glucose:validoxylamine-A 4'-O-glucosyltransferase
The enzyme, characterized from the bacterium Streptomyces hygroscopicus subsp. limoneus, catalyses the ultimate step in the biosynthesis of the antifungal agent validamycin A.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADP-alpha-D-glucose + validoxylamine A
ADP + validamycin A
-
Substrates: UDP-glucose is the most efficient glycosyl donor. Whereas GDP-glucose is less efficient, ADP-glucose iss much less efficient and TDP-glucose is the least efficient donor
Products: -
Products: -
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ADP-alpha-D-glucose + validoxylamine A
ADP + validamycin A
-
Substrates: UDP-glucose is the most efficient glycosyl donor. Whereas GDP-glucose is less efficient, ADP-glucose iss much less efficient and TDP-glucose is the least efficient donor
Products: -
Products: -
?
GDP-alpha-D-glucose + validoxylamine A
GDP + validamycin A
-
Substrates: UDP-glucose is the most efficient glycosyl donor. Whereas GDP-glucose is less efficient, ADP-glucose iss much less efficient and TDP-glucose is the least efficient donor
Products: -
Products: -
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GDP-alpha-D-glucose + validoxylamine A
GDP + validamycin A
-
Substrates: UDP-glucose is the most efficient glycosyl donor. Whereas GDP-glucose is less efficient, ADP-glucose iss much less efficient and TDP-glucose is the least efficient donor
Products: -
Products: -
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TDP-alpha-D-glucose + validoxylamine A
TDP + validamycin A
-
Substrates: UDP-glucose is the most efficient glycosyl donor. Whereas GDP-glucose is less efficient, ADP-glucose iss much less efficient and TDP-glucose is the least efficient donor
Products: -
Products: -
?
TDP-alpha-D-glucose + validoxylamine A
TDP + validamycin A
-
Substrates: UDP-glucose is the most efficient glycosyl donor. Whereas GDP-glucose is less efficient, ADP-glucose iss much less efficient and TDP-glucose is the least efficient donor
Products: -
Products: -
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UDP-alpha-D-glucose + 1,1'-bis-valienamine
UDP + validienamycin
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + 1,1'-bis-valienamine
UDP + validienamycin
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + validoxylamine A
UDP + validamycin A
-
Substrates: the role of valG in the glycosylation of validoxylamine to validamycin A is demonstrated in vitro by enzymatic assay
Products: -
Products: -
?
UDP-alpha-D-glucose + validoxylamine A
UDP + validamycin A
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + validoxylamine A
UDP + validamycin A
-
Substrates: UDP-glucose is the most efficient glycosyl donor. Whereas GDP-glucose is less efficient, ADP-glucose iss much less efficient and TDP-glucose is the least efficient donor
Products: -
Products: -
?
UDP-alpha-D-glucose + validoxylamine A
UDP + validamycin A
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + validoxylamine A
UDP + validamycin A
-
Substrates: the role of valG in the glycosylation of validoxylamine to validamycin A is demonstrated in vitro by enzymatic assay
Products: -
Products: -
?
UDP-alpha-D-glucose + validoxylamine A
UDP + validamycin A
-
Substrates: UDP-glucose is the most efficient glycosyl donor. Whereas GDP-glucose is less efficient, ADP-glucose iss much less efficient and TDP-glucose is the least efficient donor
Products: -
Products: -
?
UDP-alpha-D-glucose + validoxylamine A
UDP + validamycin A
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + validoxylamine A
UDP + validamycin A
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + validoxylamine A
UDP + validamycin A
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + validoxylamine A
UDP + validamycin A
-
Substrates: the enzyme catalyses the ultimate step in the biosynthesis of the antifungal agent validamycin A
Products: -
Products: -
?
UDP-alpha-D-glucose + validoxylamine A
UDP + validamycin A
-
Substrates: validoxylamine A i.e. (1S,2S,3R,6S)-4-(hydroxymethyl)-6-[[(1S,2S,3S,4R,5R)-2,3,4-trihydroxy-5-(hydroxymethyl)cyclohexyl]amino]cyclohex-4-ene-1,2,3-triol
Products: -
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose + 1,1'-bis-valienamine
UDP + validienamycin
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + 1,1'-bis-valienamine
UDP + validienamycin
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + validoxylamine A
UDP + validamycin A
-
Substrates: the role of valG in the glycosylation of validoxylamine to validamycin A is demonstrated in vitro by enzymatic assay
Products: -
Products: -
?
UDP-alpha-D-glucose + validoxylamine A
UDP + validamycin A
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + validoxylamine A
UDP + validamycin A
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + validoxylamine A
UDP + validamycin A
-
Substrates: the role of valG in the glycosylation of validoxylamine to validamycin A is demonstrated in vitro by enzymatic assay
Products: -
Products: -
?
UDP-alpha-D-glucose + validoxylamine A
UDP + validamycin A
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + validoxylamine A
UDP + validamycin A
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + validoxylamine A
UDP + validamycin A
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-glucose + validoxylamine A
UDP + validamycin A
-
Substrates: the enzyme catalyses the ultimate step in the biosynthesis of the antifungal agent validamycin A
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
additional information
malfunction
-
in vivo inactivation of the putative glycosyltransferase gene (valG) abolished the final attachment of glucose for validamycin A production and results in accumulation of the VAL-A precursor, validoxylamine
malfunction
-
in vivo inactivation of the putative glycosyltransferase gene (valG) abolished the final attachment of glucose for validamycin A production and results in accumulation of the VAL-A precursor, validoxylamine
-
metabolism
-
the enzyme catalyses the ultimate step in the biosynthesis of the antifungal agent validamycin A
metabolism
-
the enzyme is involved in biosynthesis of validamycin A, a weakly basic C7N-aminocyclitol-containing antibiotic
metabolism
-
ValG plays a key role in the biosynthesis of validenomycin and validomycin
metabolism
-
the enzyme is involved in biosynthesis of validamycin A, a weakly basic C7N-aminocyclitol-containing antibiotic
-
metabolism
-
ValG plays a key role in the biosynthesis of validenomycin and validomycin
-
additional information
positive effect of furfural addition on validamycin-A production
additional information
-
positive effect of furfural addition on validamycin-A production
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). VALG_STRHJ
Streptomyces hygroscopicus subsp. jinggangensis (strain 5008)
422
0
47143
Swiss-Prot
-
VLDK_STRHL
453
0
50436
Swiss-Prot
-
VLDE_STRHL
497
0
54943
Swiss-Prot
Secretory Pathway (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel affinity column chromatography, and Superdex 200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Xu, H.; Minagawa, K.; Bai, L.; Deng, Z.; Mahmud, T.
Catalytic analysis of the validamycin glycosyltransferase (ValG) and enzymatic production of 4''-epi-validamycin A
J. Nat. Prod.
71
1233-1236
2008
Streptomyces hygroscopicus subsp. limoneus
brenda
Xu, H.; Yang, J.; Bai, L.; Deng, Z.; Mahmud, T.
Genetically engineered production of 1,1-bis-valienamine and validienamycin in Streptomyces hygroscopicus and their conversion to valienamine
Appl. Microbiol. Biotechnol.
81
895-902
2009
Streptomyces hygroscopicus, Streptomyces hygroscopicus 5008
brenda
Fan, Y.; Yu, Y.; Jia, X.; Chen, X.; Shen, Y.
Cloning, expression and medium optimization of validamycin glycosyltransferase from Streptomyces hygroscopicus var. jinggangensis for the biotransformation of validoxylamine A to produce validamycin A using free resting cells
Biores. Technol.
131
13-20
2013
Streptomyces hygroscopicus, Streptomyces hygroscopicus 5008
brenda
Bai, L.; Li, L.; Xu, H.; Minagawa, K.; Yu, Y.; Zhang, Y.; Zhou, X.; Floss, H.G.; Mahmud, T.; Deng, Z.
Functional analysis of the validamycin biosynthetic gene cluster and engineered production of validoxylamine A
Chem. Biol.
13
387-397
2006
Streptomyces hygroscopicus, Streptomyces hygroscopicus 5008
brenda
Singh, D.; Kwon, H.J.; Rajkarnikar, A.; Suh, J.W.
Glucoamylase gene, vldI, is linked to validamycin biosynthesis in Streptomyces hygroscopicus var. limoneus, and vldADEFG confers validamycin production in Streptomyces lividans, revealing the role of VldE in glucose attachment
Gene
395
151-159
2007
Streptomyces hygroscopicus (Q15JG1)
brenda
Lu, Z.; Zhong, J.
Effect of furfural addition on validamycin-A production in fermentation of Streptomyces hygroscopicus 5008
Process Biochem.
92
43-48
2020
Streptomyces hygroscopicus subsp. jinggangensis (H2K893), Streptomyces hygroscopicus subsp. jinggangensis 5008 (H2K893)
-
brenda
Guo, Z.; Zhang, X.; Zhou, L.; Huang, Q.; Kang, Q.; Bai, L.
Nonglycosidic C-O bond formation catalyzed by a bifunctional pseudoglycosyltransferase ValL
Synth. Syst. Biotechnol.
10
846-857
2025
Streptomyces hygroscopicus subsp. jinggangensis, Streptomyces hygroscopicus subsp. jinggangensis TL01
brenda
EXTERNAL LINKS (specific for EC-Number 2.4.1.338)
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