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Information on EC 2.3.2.37 - ergosteryl-3beta-O-L-aspartate synthase
for references in articles please use BRENDA:EC2.3.2.37
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.2 Aminoacyltransferases
2.3.2.37 ergosteryl-3beta-O-L-aspartate synthase
IUBMB Comments
The enzyme, detected in fungal species that belong to the Ascomycota and Basidiomycota phyla and characterized from Aspergillus fumigatus, is bifunctional. The AspRS domain catalyses the transfer of L-aspartate to tRNAAsp (EC 6.1.1.12), while the second domain carries out the transfer of L-aspartate to the 3β-hydroxyl of ergosterol.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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1-(ergostan-3beta-yl)-L-aspartate
Synonyms
AFUA_1g02570, AO090005000838, AspRS-DUF2156, AspRS-DUF2156 protein, DUF2156 domain protein, ErdS, Erg-Asp synthase, ergosteryl-3beta-O-L-aspartate synthase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AFUA_1g02570
AO090005000838
AspRS-DUF2156
AspRS-DUF2156 protein
DUF2156 domain protein
ErdS
Erg-Asp synthase
ergosteryl-3beta-O-L-aspartate synthase
ErdS
-
the bifunctional enzyme corresponds to a unique fusion of an aspartyl-tRNA synthetase that produces Asp-tRNAAsp, and of a domain of unknown function, which actually transfers aspartate from Asp-tRNAAsp onto ergosterol
ErdS
-
the bifunctional enzyme corresponds to a unique fusion of an aspartyl-tRNA synthetase that produces Asp-tRNAAsp, and of a domain of unknown function, which actually transfers aspartate from Asp-tRNAAsp onto ergosterol
ErdS
-
the bifunctional enzyme corresponds to a unique fusion of an aspartyl-tRNA synthetase that produces Asp-tRNAAsp, and of a domain of unknown function, which actually transfers aspartate from Asp-tRNAAsp onto ergosterol
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-aspartyl-tRNAAsp + ergosterol = tRNAAsp + 1-(ergostan-3beta-yl)-L-aspartate
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SYSTEMATIC NAME
IUBMB Comments
L-aspartyl-tRNAAsp:ergosterol-3beta-O-L-aspartate synthase
The enzyme, detected in fungal species that belong to the Ascomycota and Basidiomycota phyla and characterized from Aspergillus fumigatus, is bifunctional. The AspRS domain catalyses the transfer of L-aspartate to tRNAAsp (EC 6.1.1.12), while the second domain carries out the transfer of L-aspartate to the 3beta-hydroxyl of ergosterol.
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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
ATP + Asp + ergosterol
AMP + diphosphate + ergosteryl-3beta-O-L-aspartate
Substrates: -
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ATP + Asp + ergosterol
AMP + diphosphate + ergosteryl-3beta-O-L-aspartate
Substrates: -
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ATP + Asp + ergosterol
AMP + diphosphate + ergosteryl-3beta-O-L-aspartate
Substrates: -
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ATP + Asp + ergosterol
AMP + diphosphate + ergosteryl-3beta-O-L-aspartate
Substrates: -
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ATP + Asp + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
Substrates: -
Products: -
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ATP + Asp + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
Substrates: -
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ATP + Asp + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
Substrates: -
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ATP + Asp + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
Substrates: -
Products: -
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ATP + L-Asp + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
Substrates: cf. EC 6.1.1.12
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ATP + L-Asp + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
Substrates: cf. EC 6.1.1.12
Products: -
Products: -
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ATP + L-Asp + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
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Substrates: cf. EC 6.1.1.12
Products: -
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ATP + L-aspartate + ergosterol
AMP + diphosphate + ergosteryl-3beta-O-L-aspartate
Substrates: -
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ATP + L-aspartate + ergosterol
AMP + diphosphate + ergosteryl-3beta-O-L-aspartate
Substrates: -
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ergosterol + L-aspartyl-tRNAAsp
ergosteryl-3beta-O-L-aspartate + tRNAAsp
Substrates: -
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ergosterol + L-aspartyl-tRNAAsp
ergosteryl-3beta-O-L-aspartate + tRNAAsp
Substrates: -
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ergosterol + L-aspartyl-tRNAAsp
ergosteryl-3beta-O-L-aspartate + tRNAAsp
Substrates: -
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ergosterol + L-aspartyl-tRNAAsp
ergosteryl-3beta-O-L-aspartate + tRNAAsp
Substrates: -
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L-aspartyl-tRNAAsp + ergosterol
tRNAAsp + 1-(ergostan-3beta-yl)-L-aspartate
Substrates: -
Products: -
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L-aspartyl-tRNAAsp + ergosterol
tRNAAsp + 1-(ergostan-3beta-yl)-L-aspartate
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Substrates: -
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L-aspartyl-tRNAAsp + ergosterol
tRNAAsp + 1-(ergostan-3beta-yl)-L-aspartate
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Substrates: the enzyme is highly specific for L-aspartyl-tRNAAsp
Products: -
Products: -
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L-aspartyl-tRNAAsp + ergosterol
tRNAAsp + 1-(ergostan-3beta-yl)-L-aspartate
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Substrates: -
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L-aspartyl-tRNAAsp + ergosterol
tRNAAsp + 1-(ergostan-3beta-yl)-L-aspartate
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Substrates: the enzyme is highly specific for L-aspartyl-tRNAAsp
Products: -
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L-aspartyl-tRNAAsp + ergosterol
tRNAAsp + 1-(ergostan-3beta-yl)-L-aspartate
Substrates: -
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Products: -
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L-aspartyl-tRNAAsp + ergosterol
tRNAAsp + 1-(ergostan-3beta-yl)-L-aspartate
-
Substrates: -
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L-aspartyl-tRNAAsp + ergosterol
tRNAAsp + 1-(ergostan-3beta-yl)-L-aspartate
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Substrates: the enzyme is highly specific for L-aspartyl-tRNAAsp
Products: -
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L-aspartyl-tRNAAsp + ergosterol
tRNAAsp + 1-(ergostan-3beta-yl)-L-aspartate
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Substrates: -
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additional information
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Substrates: a bifunctional enzyme, ergosteryl-3beta-O-L-aspartate synthase ErdS, is responsible for synthesis of ergosteryl-3beta-O-L-aspartate. ErdS produces aspartyl-tRNAAsp, reaction of EC 6.1.1.12, and transfers aspartate from Asp-tRNAAsp onto ergosterol
Products: -
Products: -
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additional information
?
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Substrates: a bifunctional enzyme, ergosteryl-3beta-O-L-aspartate synthase ErdS, is responsible for synthesis of ergosteryl-3beta-O-L-aspartate. ErdS produces aspartyl-tRNAAsp, reaction of EC 6.1.1.12, and transfers aspartate from Asp-tRNAAsp onto ergosterol
Products: -
Products: -
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additional information
?
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Substrates: the enzyme ErdS produces its own Asp-tRNAAsp from ATP, L-Asp, and tRNAAsp, and the cis-acting transferase (DUF2156) domain uses it to transfer L-Asp onto ergosterol
Products: -
Products: -
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additional information
?
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Substrates: a bifunctional enzyme, ergosteryl-3beta-O-L-aspartate synthase ErdS, is responsible for synthesis of ergosteryl-3beta-O-L-aspartate. ErdS produces aspartyl-tRNAAsp, reaction of EC 6.1.1.12, and transfers aspartate from Asp-tRNAAsp onto ergosterol
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme ErdS produces its own Asp-tRNAAsp from ATP, L-Asp, and tRNAAsp, and the cis-acting transferase (DUF2156) domain uses it to transfer L-Asp onto ergosterol
Products: -
Products: -
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additional information
?
-
-
Substrates: a bifunctional enzyme, ergosteryl-3beta-O-L-aspartate synthase ErdS, is responsible for synthesis of ergosteryl-3beta-O-L-aspartate. ErdS produces aspartyl-tRNAAsp, reaction of EC 6.1.1.12, and transfers aspartate from Asp-tRNAAsp onto ergosterol
Products: -
Products: -
?
additional information
?
-
Substrates: a bifunctional enzyme, ergosteryl-3beta-O-L-aspartate synthase ErdS, is responsible for synthesis of ergosteryl-3beta-O-L-aspartate. ErdS produces aspartyl-tRNAAsp, reaction of EC 6.1.1.12, and transfers aspartate from Asp-tRNAAsp onto ergosterol
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme ErdS produces its own Asp-tRNAAsp from ATP, L-Asp, and tRNAAsp, and the cis-acting transferase (DUF2156) domain uses it to transfer L-Asp onto ergosterol
Products: -
Products: -
-
additional information
?
-
Substrates: a bifunctional enzyme, ergosteryl-3beta-O-L-aspartate synthase ErdS, is responsible for synthesis of ergosteryl-3beta-O-L-aspartate. ErdS produces aspartyl-tRNAAsp, reaction of EC 6.1.1.12, and transfers aspartate from Asp-tRNAAsp onto ergosterol
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
ATP + Asp + ergosterol
AMP + diphosphate + ergosteryl-3beta-O-L-aspartate
Substrates: -
Products: -
Products: -
?
ATP + Asp + ergosterol
AMP + diphosphate + ergosteryl-3beta-O-L-aspartate
Substrates: -
Products: -
Products: -
?
ATP + Asp + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
Substrates: -
Products: -
Products: -
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ATP + Asp + tRNAAsp
AMP + diphosphate + L-aspartyl-tRNAAsp
Substrates: -
Products: -
Products: -
?
ergosterol + L-aspartyl-tRNAAsp
ergosteryl-3beta-O-L-aspartate + tRNAAsp
Substrates: -
Products: -
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ergosterol + L-aspartyl-tRNAAsp
ergosteryl-3beta-O-L-aspartate + tRNAAsp
Substrates: -
Products: -
Products: -
?
L-aspartyl-tRNAAsp + ergosterol
tRNAAsp + 1-(ergostan-3beta-yl)-L-aspartate
Substrates: -
Products: -
Products: -
?
L-aspartyl-tRNAAsp + ergosterol
tRNAAsp + 1-(ergostan-3beta-yl)-L-aspartate
-
Substrates: -
Products: -
Products: -
?
L-aspartyl-tRNAAsp + ergosterol
tRNAAsp + 1-(ergostan-3beta-yl)-L-aspartate
-
Substrates: -
Products: -
Products: -
?
L-aspartyl-tRNAAsp + ergosterol
tRNAAsp + 1-(ergostan-3beta-yl)-L-aspartate
Substrates: -
Products: -
Products: -
?
L-aspartyl-tRNAAsp + ergosterol
tRNAAsp + 1-(ergostan-3beta-yl)-L-aspartate
-
Substrates: -
Products: -
Products: -
?
L-aspartyl-tRNAAsp + ergosterol
tRNAAsp + 1-(ergostan-3beta-yl)-L-aspartate
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: a bifunctional enzyme, ergosteryl-3beta-O-L-aspartate synthase ErdS, is responsible for synthesis of ergosteryl-3beta-O-L-aspartate. ErdS produces aspartyl-tRNAAsp, reaction of EC 6.1.1.12, and transfers aspartate from Asp-tRNAAsp onto ergosterol
Products: -
Products: -
?
additional information
?
-
Substrates: a bifunctional enzyme, ergosteryl-3beta-O-L-aspartate synthase ErdS, is responsible for synthesis of ergosteryl-3beta-O-L-aspartate. ErdS produces aspartyl-tRNAAsp, reaction of EC 6.1.1.12, and transfers aspartate from Asp-tRNAAsp onto ergosterol
Products: -
Products: -
?
additional information
?
-
Substrates: a bifunctional enzyme, ergosteryl-3beta-O-L-aspartate synthase ErdS, is responsible for synthesis of ergosteryl-3beta-O-L-aspartate. ErdS produces aspartyl-tRNAAsp, reaction of EC 6.1.1.12, and transfers aspartate from Asp-tRNAAsp onto ergosterol
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
evolution
metabolism
physiological function
evolution
ErdS corresponds to a unique fusion of an aspartyl-tRNA synthetase that produces aspartyl-tRNAAsp and of a Domain of Unknown Function 2156, which actually transfers aspartate from Asp-tRNAAsp onto ergosterol. The entire ergosteryl-3beta-O-L-aspartate synthesis/degradation pathway is conserved across higher fungi
evolution
ErdS corresponds to a unique fusion of an aspartyl-tRNA synthetase that produces aspartyl-tRNAAsp and of a Domain of Unknown Function 2156, which actually transfers aspartate from Asp-tRNAAsp onto ergosterol. The entire ergosteryl-3beta-O-L-aspartate synthesis/degradation pathway is conserved across higher fungi
evolution
-
ErdS corresponds to a unique fusion of an aspartyl-tRNA synthetase that produces aspartyl-tRNAAsp and of a Domain of Unknown Function 2156, which actually transfers aspartate from Asp-tRNAAsp onto ergosterol. The entire ergosteryl-3beta-O-L-aspartate synthesis/degradation pathway is conserved across higher fungi
-
evolution
-
ErdS corresponds to a unique fusion of an aspartyl-tRNA synthetase that produces aspartyl-tRNAAsp and of a Domain of Unknown Function 2156, which actually transfers aspartate from Asp-tRNAAsp onto ergosterol. The entire ergosteryl-3beta-O-L-aspartate synthesis/degradation pathway is conserved across higher fungi
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metabolism
-
the enzyme is essential for the synthesis of lipid X. In the full-length enzyme, the DUF2156 domain likely transfers Asp from Asp-tRNAAsp onto an accepting lipid, thereby decreasing the amount of Asp-tRNAAsp available for protein synthesis and impacting growth
metabolism
the enzyme is essential for the synthesis of lipid X. In the full-length enzyme, the DUF2156 domain likely transfers Asp from Asp-tRNAAsp onto an accepting lipid, thereby decreasing the amount of Asp-tRNAAsp available for protein synthesis and impacting growth
metabolism
the enzyme is essential for the synthesis of lipid X. In the full-length enzyme, the DUF2156 domain likely transfers Asp from Asp-tRNAAsp onto an accepting lipid, thereby decreasing the amount of Asp-tRNAAsp available for protein synthesis and impacting growth
physiological function
ergosteryl-3beta-O-L-aspartate is a type of sterol conjugate, specific to fungi, that is produced by ErdSs enzymes, through a tRNA-dependent process. Fusion of the AspRS and the transferase (DUF2156) domain is required for full activity. ErdS mutants grow normally on solid media. Removal of the Asp group from ergosteryl-3beta-O-L-aspartate is catalyzed by a second enzyme, ErdH, that is a ergosteryl-3beta-O-L-aspartate hydrolase participating in the turnover of the conjugated sterol in vivo
physiological function
ergosteryl-3beta-O-L-aspartate is a type of sterol conjugate, specific to fungi, that is produced by ErdS enzymes, through a tRNA-dependent process. Fusion of the AspRS and the transferase (DUF2156) domain is required for full activity. ErdS mutants grow normally on solid media. Removal of the Asp group from ergosteryl-3beta-O-L-aspartate is catalyzed by a second enzyme, ErdH, that is a ergosteryl-3beta-O-L-aspartate hydrolase participating in the turnover of the conjugated sterol in vivo
physiological function
-
ergosteryl-3beta-O-L-aspartate is a type of sterol conjugate, specific to fungi, that is produced by ErdSs enzymes, through a tRNA-dependent process. Fusion of the AspRS and the transferase (DUF2156) domain is required for full activity. ErdS mutants grow normally on solid media. Removal of the Asp group from ergosteryl-3beta-O-L-aspartate is catalyzed by a second enzyme, ErdH, that is a ergosteryl-3beta-O-L-aspartate hydrolase participating in the turnover of the conjugated sterol in vivo
-
physiological function
-
ergosteryl-3beta-O-L-aspartate is a type of sterol conjugate, specific to fungi, that is produced by ErdS enzymes, through a tRNA-dependent process. Fusion of the AspRS and the transferase (DUF2156) domain is required for full activity. ErdS mutants grow normally on solid media. Removal of the Asp group from ergosteryl-3beta-O-L-aspartate is catalyzed by a second enzyme, ErdH, that is a ergosteryl-3beta-O-L-aspartate hydrolase participating in the turnover of the conjugated sterol in vivo
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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). Q2URG4_ASPOR
Aspergillus oryzae (strain ATCC 42149 / RIB 40)
954
0
108303
TrEMBL
-
Q4WKG3_ASPFU
Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)
947
0
107922
TrEMBL
-
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yakobov, N.; Fischer, F.; Mahmoudi, N.; Saga, Y.; Grube, C.D.; Roy, H.; Senger, B.; Grob, G.; Tatematsu, S.; Yokokawa, D.; Mouyna, I.; Latge, J.-P.; Nakajima, H.; Kushiro, T.; Becker, H.D.
RNA-dependent sterol aspartylation in fungi
Proc. Natl. Acad. Sci. USA
117
14948-14957
2020
Aspergillus fumigatus, Aspergillus fumigatus (Q4WKG3), Aspergillus fumigatus ATCC MYA-4609 (Q4WKG3), Aspergillus oryzae, Aspergillus oryzae (Q2URG4), Aspergillus oryzae ATCC 42149 (Q2URG4), Neurospora crassa
brenda
Yakobov, N.; Mahmoudi, N.; Grob, G.; Yokokawa, D.; Saga, Y.; Kushiro, T.; Worrell, D.; Roy, H.; Schaller, H.; Senger, B.; Huck, L.; Riera Gascon, G.; Becker, H.D.; Fischer, F.
RNA-dependent synthesis of ergosteryl-3beta-O-glycine in Ascomycota expands the diversity of steryl-amino acids
J. Biol. Chem.
298
101657
2022
Aspergillus fumigatus, Aspergillus fumigatus CEA17, Aspergillus oryzae, no activity in Saccharomyces cerevisiae
brenda
EXTERNAL LINKS (specific for EC-Number 2.3.2.37)
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