Any feedback?
No. of entries
Information on EC 2.3.1.190 - acetoin dehydrogenase system
for references in articles please use BRENDA:EC2.3.1.190
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.190 acetoin dehydrogenase system
IUBMB Comments
Requires thiamine diphosphate. It belongs to the 2-oxoacid dehydrogenase system family, which also includes EC 1.2.1.104, pyruvate dehydrogenase system, EC 1.2.1.105, 2-oxoglutarate dehydrogenase system, EC 1.2.1.25, branched-chain α-keto acid dehydrogenase system, and EC 1.4.1.27, glycine cleavage system. With the exception of the glycine cleavage system, which contains 4 components, the 2-oxoacid dehydrogenase systems share a common structure, consisting of three main components, namely a 2-oxoacid dehydrogenase (E1), a dihydrolipoamide acyltransferase (E2), and dihydrolipoamide dehydrogenase (E3).
The expected taxonomic range for this enzyme is: Bacteria, Archaea
- 2.3.1.190
- dihydrolipoamide
-
alcaligenes
- carbinolicus
-
catabolite
-
pelobacter
- eutrophus
- magnum
-
dissimilation
- 2,3-butanediol
- synthesis
showSynonyms
acetoin dehydrogenase, acetoin dehydrogenase enzyme system, ao:dcpip or, aodh es, acetoin dehydrogenase complex, acetoin dehydrogenase e1, pa4150, acetoin dehydrogenase system, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetoin dehydrogenase
-
-
-
-
acetoin dehydrogenase complex
-
-
-
-
acetoin dehydrogenase E1
acetoin dehydrogenase enzyme system
AcoAB
AdhA
AdhB
AdhC
AdhD
AoDH ES
-
-
-
-
PA4150
PA4151
acetoin dehydrogenase enzyme system
Q9HWN1; Q9HWN0
consists of TPP-dependent acetoin dehydrogenase (AoDH E1), dihydrolipoamide acetyltransferase (AoDH E2) and dihydrolipoamide dehydrogenase (AoDH E3)
acetoin dehydrogenase enzyme system
Q9HWN1; Q9HWN0
consists of TPP-dependent acetoin dehydrogenase (AoDH E1), dihydrolipoamide acetyltransferase (AoDH E2) and dihydrolipoamide dehydrogenase (AoDH E3)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetoin + CoA + NAD+ = acetaldehyde + acetyl-CoA + NADH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:acetoin O-acetyltransferase
Requires thiamine diphosphate. It belongs to the 2-oxoacid dehydrogenase system family, which also includes EC 1.2.1.104, pyruvate dehydrogenase system, EC 1.2.1.105, 2-oxoglutarate dehydrogenase system, EC 1.2.1.25, branched-chain alpha-keto acid dehydrogenase system, and EC 1.4.1.27, glycine cleavage system. With the exception of the glycine cleavage system, which contains 4 components, the 2-oxoacid dehydrogenase systems share a common structure, consisting of three main components, namely a 2-oxoacid dehydrogenase (E1), a dihydrolipoamide acyltransferase (E2), and dihydrolipoamide dehydrogenase (E3).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetoin + 2,6-dichlorophenolindophenol
acetaldehyde + ?
Substrates: E1 complex
Products: -
Products: -
?
acetoin + 2,6-dichlorophenolindophenol
acetaldehyde + ?
Substrates: E1 complex
Products: -
Products: -
?
acetoin + 2,6-dichlorophenolindophenol
acetaldehyde + ?
-
Substrates: -
Products: -
Products: -
?
acetoin + CoA + NAD+
acetaldehyde + acetyl-CoA + NADH + H+
Q9HWN1; Q9HWN0
Substrates: -
Products: -
Products: -
?
acetoin + CoA + NAD+
acetaldehyde + acetyl-CoA + NADH + H+
Q9HWN1; Q9HWN0
Substrates: -
Products: -
Products: -
?
diacetyl + 2,6-dichlorophenolindophenol
?
Substrates: E1 complex, 59% of the activity with acetoin
Products: -
Products: -
?
diacetyl + 2,6-dichlorophenolindophenol
?
-
Substrates: -
Products: -
Products: -
?
diacetyl + CoA + NAD+
?
Q9HWN1; Q9HWN0
Substrates: -
Products: -
Products: -
?
methyl acetoin + 2,6-dichlorophenolindophenol
? + ?
Substrates: E1 complex, 107% of the activity with acetoin
Products: -
Products: -
?
methyl acetoin + 2,6-dichlorophenolindophenol
? + ?
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: no detectable activity with 2-oxoglutarate, pyruvate or the branched-chain 2-oxoacids, 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate
Products: -
Products: -
?
additional information
?
-
Substrates: no detectable activity with 2-oxoglutarate, pyruvate or the branched-chain 2-oxoacids, 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no detectable activity with 2-oxoglutarate, pyruvate or the branched-chain 2-oxoacids, 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate
Products: -
Products: -
?
additional information
?
-
-
Substrates: The combination of purified Ao:DCPIP OR, dihydrolipoamide dehydrogenase, and dihydrolipoamide acetyltransferase in the presence of thiamine diphosphate and the substrate acetoin or methylacetoin results in a coenzyme A-dependent reduction of NAD+
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
Substrates: The combination of purified Ao:DCPIP OR, dihydrolipoamide dehydrogenase, and dihydrolipoamide acetyltransferase in the presence of thiamine diphosphate and the substrate acetoin or methylacetoin results in a coenzyme A-dependent reduction of NAD+
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
A0A031WDC0 i.e. acetoin dehydrogenase E1 component AcoA, A0A031WD22 i.e. 2-oxoisovalerate dehydrogenase subunit AcoB
A0A031WDC0; A0A031WD22
UniProt
brenda
Q8DWD7 i.e. E1 component alpha-subunit AdhA, Q8DWD6 i.e. E1 component beta-subunit AdhB, Q8DWD5 i.e. dihydrolipoamide acetyltransferase component AdhC, Q8DWD4 i.e. dihydrolipoyl dehydrogenase AdhD
Q8DWD7; Q8DWD6; Q8DWD5; Q8DWD4
UniProt
brenda
Q8DWD7 i.e. E1 component alpha-subunit AdhA, Q8DWD6 i.e. E1 component beta-subunit AdhB, Q8DWD5 i.e. dihydrolipoamide acetyltransferase component AdhC, Q8DWD4 i.e. dihydrolipoyl dehydrogenase AdhD
Q8DWD7; Q8DWD6; Q8DWD5; Q8DWD4
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
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
malfunction
metabolism
physiological function
additional information
-
disruption of the gene acoA encoding subunit E1alpha results in strains impaired in expression of dephosphate-dependent E1 activity, to remove acetoin from the medium and to grow with acetoin as sole carbon source
malfunction
Q9HWN1; Q9HWN0
acoA, acoB are knocked out individually in Pseudomonas aeruginosa PAO1. The mutants lose the ability to grow in acetoin or 2,3-butanediol
malfunction
-
acoA, acoB are knocked out individually in Pseudomonas aeruginosa PAO1. The mutants lose the ability to grow in acetoin or 2,3-butanediol
-
metabolism
-
the enzyme is involved in the degradation of the sulfonylurea herbicide nicosulfuron
metabolism
Q9HWN1; Q9HWN0
the enzyme is involved in 2,3-butanediol catabolism
metabolism
-
the enzyme is involved in 2,3-butanediol catabolism
-
metabolism
Bacillus subtilis YB10
-
the enzyme is involved in the degradation of the sulfonylurea herbicide nicosulfuron
-
physiological function
-
the acetoin dehydrogenase enzyme system is responsible for R-acetoin dissimilation. Mutants lose the ability to grow on acetoin as the sole carbon source, and the acetoin accumulated cannot be dissimilated. In the presence of another carbon source, the acetoin accumulated in broth of acetoin dehydrogenase mutants is converted to 2,3-butanediol
physiological function
A0A031WDC0; A0A031WD22
an acoA null mutant produces significantly more spores and initiates sporulation earlier than the wild-type. Growth and culture density of Clostridioides difficile is not increased by acetoin availability or disruption of the aco pathway
physiological function
Q8DWD7; Q8DWD6; Q8DWD5; Q8DWD4
deletion mutations of Adh genes confers oxygen-dependent sensitivity to slightly alkaline pH (pH 7.2-7.6), and lead to growth defects when glucose or sucrose serve as major carbon sources. Supplementation of media with 0.5% pyruvate improves growth of Adh mutants. Subunit AdhC interacts with transcription factor SpxA2
physiological function
-
deletion mutations of Adh genes confers oxygen-dependent sensitivity to slightly alkaline pH (pH 7.2-7.6), and lead to growth defects when glucose or sucrose serve as major carbon sources. Supplementation of media with 0.5% pyruvate improves growth of Adh mutants. Subunit AdhC interacts with transcription factor SpxA2
-
physiological function
-
the acetoin dehydrogenase enzyme system is responsible for R-acetoin dissimilation. Mutants lose the ability to grow on acetoin as the sole carbon source, and the acetoin accumulated cannot be dissimilated. In the presence of another carbon source, the acetoin accumulated in broth of acetoin dehydrogenase mutants is converted to 2,3-butanediol
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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). ACOA_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
333
0
35375
Swiss-Prot
other Location (Reliability: 1)
ACOB_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
338
0
35960
Swiss-Prot
Secretory Pathway (Reliability: 5)
Q97YF5_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
332
0
36565
TrEMBL
Secretory Pathway (Reliability: 4)
Q97YF6_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
345
0
38371
TrEMBL
other Location (Reliability: 2)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
138000
-
gel filtration, component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase, exhibits tetrameric alpha2beta2 structure, with alpha, 35243 Da and beta, 35788 Da, calculated and SDS-PAGE
additional information
component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase, exhibits tetrameric alpha2beta2 structure, with alpha, 35243 Da and beta, 35788 Da, calculated and SDS-PAGE
additional information
-
component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase, exhibits tetrameric alpha2beta2 structure, with alpha, 38500 and beta, 34000 Da, SDS-PAGE
additional information
component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase, exhibits tetrameric alpha2beta2 structure, with alpha, 43000 and beta, 33000 Da, SDS-PAGE
additional information
component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase, exhibits tetrameric alpha2beta2 structure, with alpha, 43000 and beta, 33000 Da, SDS-PAGE
additional information
-
component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase, exhibits tetrameric alpha2beta2 structure, with alpha, 43000 and beta, 33000 Da, SDS-PAGE
additional information
-
component E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase, exhibits tetrameric alpha2beta2 structure, with alpha, 37500 Da, and beta, 38500 Da, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acylation
acylation
Q8DWD7; Q8DWD6; Q8DWD5; Q8DWD4
the E3 AdhD subunit bears an N-terminal lipoylation domain. Changing the lipoyl domains of AdhC and AdhD, causes no significant reduction in pH sensitivity. The AdhD K43R mutation eliminating the lipoylation site results in an observable growth defect in glucose medium
acylation
-
the E3 AdhD subunit bears an N-terminal lipoylation domain. Changing the lipoyl domains of AdhC and AdhD, causes no significant reduction in pH sensitivity. The AdhD K43R mutation eliminating the lipoylation site results in an observable growth defect in glucose medium
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K43R
K43R
Q8DWD7; Q8DWD6; Q8DWD5; Q8DWD4
mutation in subunit AdhD, eliminating the lipoylation site. The mutation results in an observable growth defect in glucose medium
K43R
-
mutation in subunit AdhD, eliminating the lipoylation site. The mutation results in an observable growth defect in glucose medium
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from acetoin-grown cells
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of the acetoin dehydrogenase operon, acoRABCL, is pH-dependent and regulated by acetoin
A0A031WDC0; A0A031WD22
formation of the enzyme components of the acetoin dehydrogenase enzyme system E1, i.e. acetoin:2,6-dichlorophenolindophenol oxidoreductase Ao:DCPIP OR,, E2, i.e. dihydrolipoamide acetyltransferase DHLTA, and E3, i.e. dihydrolipoamide dehydrogenase DHLDH, are induced during growth on acetoin
-
the enzymes Ao:DCPIP OR, dihydrolipoamide dehydrogenase, and dihydrolipoamide acetyltransferase are induced during growth on acetoin, whereas they are absent or scarcely present in cells grown on a nonacetoinogenic substrate
-
transcriptions of the aco operon and acoR are repressed by glucose via CcpA, and CcpA specifically bound to sequences within the acoR promoter fragment
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
engineering a budC acoABCD double mutant, which has lost 2,3-butanediol dehydrogenase activity and the acetoin dehydrogenase system for R-acetoin production. Optimized conditions include aerobic batch culture and mildly acidic conditions. 62.3 g per l R-acetoin can be produced by budC and acoABCD double mutants in 57 h culture, with an optical purity of 98.0%, and a substrate conversion ratio of 28.7%
synthesis
-
engineering a budC acoABCD double mutant, which has lost 2,3-butanediol dehydrogenase activity and the acetoin dehydrogenase system for R-acetoin production. Optimized conditions include aerobic batch culture and mildly acidic conditions. 62.3 g per l R-acetoin can be produced by budC and acoABCD double mutants in 57 h culture, with an optical purity of 98.0%, and a substrate conversion ratio of 28.7%
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Oppermann, F.B.; Schmidt, B.; Steinbuchel, A.
Purification and characterization of acetoin:2,6-dichlorophenolindophenol oxidoreductase, dihydrolipoamide dehydrogenase, and dihydrolipoamide acetyltransferase of the Pelobacter carbinolicus acetoin dehydrogenase enzyme system
J. Bacteriol.
173
757-767
1991
Syntrophotalea carbinolica
brenda
Lorenzl, H.; Oppermann, F.; Schmidt, B.; Steinbuchel, A.
Purification and characterization of the E1 component of the Clostridium magnum acetoin dehydrogenase enzyme system
Antonie van Leeuwenhoek
64
9-15
1993
Clostridium magnum
brenda
Payne, K.A.; Hough, D.W.; Danson, M.J.
Discovery of a putative acetoin dehydrogenase complex in the hyperthermophilic archaeon Sulfolobus solfataricus
FEBS Lett.
584
1231-1234
2010
Saccharolobus solfataricus (Q97YF6), Saccharolobus solfataricus (Q97YF5), Saccharolobus solfataricus
brenda
Huang, M.; Oppermann, F.B.; Steinbuechel, A.
Molecular characterization of the Pseudomonas putida 2,3-butanediol catabolic pathway
FEMS Microbiol. Lett.
124
141-150
1994
Pseudomonas putida (Q52014), Pseudomonas putida (Q52015), Pseudomonas putida
brenda
Priefert, H.; Hein, S.; Krueger, N.; Zeh, K.; Schmidt, B.; Steinbuechel, A.
Identification and molecular characterization of the Alcaligenes eutrophus H16 aco operon genes involved in acetoin catabolism
J. Bacteriol.
173
4056-4071
1991
Alcaligenes eutrophus H16 (P27745), Alcaligenes eutrophus H16 (P27746)
brenda
Krueger, N.; Oppermann, F.B.; Lorenzl, H.; Steinbuechel, A.
Biochemical and molecular characterization of the Clostridium magnum acetoin dehydrogenase enzyme system
J. Bacteriol.
176
3614-3630
1994
Clostridium magnum (Q46143), Clostridium magnum (Q46142), Clostridium magnum
brenda
Huang, M.; Oppermann-Sanio, F.B.; Steinbuechel, A.
Biochemical and molecular characterization of the Bacillus subtilis acetoin catabolic pathway
J. Bacteriol.
181
3837-3841
1999
Bacillus subtilis
brenda
Wang, D.; Zhou, J.; Chen, C.; Wei, D.; Shi, J.; Jiang, B.; Liu, P.; Hao, J.
R-acetoin accumulation and dissimilation in Klebsiella pneumoniae
J. Ind. Microbiol. Biotechnol.
42
1105-1115
2015
Klebsiella pneumoniae, Klebsiella pneumoniae CGMCC 1.6366
brenda
Liu, Q.; Liu, Y.; Kang, Z.; Xiao, D.; Gao, C.; Xu, P.; Ma, C.
2,3-Butanediol catabolism in Pseudomonas aeruginosa PAO1
Environ. Microbiol.
20
3927-3940
2018
Pseudomonas aeruginosa (Q9HWN1 AND Q9HWN0), Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692 (Q9HWN1 AND Q9HWN0)
brenda
Zhang, Z.; Zhang, Y.; Yang, D.C.; Zhang, J.L.
Expression and functional analysis of three nicosulfuron-degrading enzymes from Bacillus subtilis YB1
J. Environ. Sci. Health B
53
476-485
2018
Bacillus subtilis, Bacillus subtilis YB10
brenda
Peng, Q.; Zhao, X.; Wen, J.; Huang, M.; Zhang, J.; Song, F.
Transcription in the acetoin catabolic pathway is regulated by AcoR and CcpA in Bacillus thuringiensis
Microbiol. Res.
235
126438
2020
Bacillus thuringiensis
brenda
Wetzel, D.; Rizvi, A.; Edwards, A.N.; McBride, S.M.
The predicted acetoin dehydrogenase pathway represses sporulation of Clostridioides difficile
BioRxiv
FEHLT
0000
2023
Clostridioides difficile (A0A031WDC0 and A0A031WD22)
brenda
Zuber, P.; Nakano, M.M.; Kajfasz, J.K.; Lemos, J.A.
Disruption of the adh (acetoin dehydrogenase) operon has wide-ranging effects on Streptococcus mutans growth and stress response
J. Bacteriol.
204
e0057821
2022
Streptococcus mutans (Q8DWD7 and Q8DWD6 and Q8DWD5 and Q8DWD4), Streptococcus mutans UA159 (Q8DWD7 and Q8DWD6 and Q8DWD5 and Q8DWD4)
brenda
EXTERNAL LINKS (specific for EC-Number 2.3.1.190)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
