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Information on EC 6.3.2.26 - N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase
for references in articles please use BRENDA:EC6.3.2.26
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EC Tree 6 Ligases
6.3 Forming carbon-nitrogen bonds
6.3.2 Acid—amino-acid ligases (peptide synthases)
6.3.2.26 N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase
IUBMB Comments
Requires Mg2+. The enzyme contains 4′-phosphopantetheine, which may be involved in the mechanism of the reaction. Forms part of the penicillin biosynthesis pathway (for pathway, click here).
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 6.3.2.26
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delta-l-alpha-aminoadipyl-l-cysteinyl-d-valine
- penicillin
- chrysogenum
- clavuligerus
- acremonium
- beta-lactams
- synthetases
- tripeptide
- nidulans
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pcbab
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cephalosporium
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cephamycins
- pantoate
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gramicidin
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epimerization
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lld-acv
- 4'-phosphopantothenate
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l-alpha-aminoadipic
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non-ribosomal
- kodakarensis
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epsilon-aminotransferase
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thiotemplate
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tyrocidine
- biotechnology
- medicine
Reaction Schemes
showSynonyms
acv synthetase, delta-(l-alpha-aminoadipyl)-l-cysteinyl-d-valine synthetase, phosphopantothenate synthetase, tk1686, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACV synthetase
ACVS
DELTA-(alpha-aminoadipyl)cysteinylvaline synthetase
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delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-valine synthetase
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delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase
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delta-(L-alpha-aminoadipyl-L-cysteinyl-D-valine synthetase)
delta-L-(alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase
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L-(alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase
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L-delta-(alpha-aminoadipoyl)-L-cysteinyl-D-valine synthetase
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synthetase, delta-(alpha-aminoadipyl)cysteinylvaline
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ACV synthetase
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delta-(L-alpha-aminoadipyl-L-cysteinyl-D-valine synthetase)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O = 3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylic acid amid formation
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peptide bond formation
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PATHWAY SOURCE
PATHWAYS
MetaCyc
isopenicillin N biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
L-2-aminohexanedioate:L-cysteine:L-valine ligase (AMP-forming, valine-inverting)
Requires Mg2+. The enzyme contains 4'-phosphopantetheine, which may be involved in the mechanism of the reaction. Forms part of the penicillin biosynthesis pathway (for pathway, click here).
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CAS REGISTRY NUMBER
COMMENTARY
57219-73-5
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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
3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O
3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
6-oxopiperidine 2-carboxylic acid + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
alpha-aminoadipic acid + L-valine + L-lysine + ?
L-delta-alpha-aminoadipyl-L-cysteinyl-D-valine + ?
-
Substrates: enzyme is a nonribosomal peptide synthetase (NRPS) able to form ribosome-independent peptide bonds
Products: ACV
Products: ACV
?
DL-valine + L-O-(methylserine) + L-2-aminohexanedioate + ATP
L-O-(methylserinyl)-D-valine + L-O-(methylserinyl)-D-valine + AMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
L-2-aminoadipate + allylglycine + L-valine + ATP
L-delta-(aminoadipyl)-L-allylglycinyl-D-valine + AMP + diphosphate
L-2-aminoadipate + L-cystathionine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
L-2-aminoadipate + L-cysteine + L-allo-isoleucine + ATP
L-delta-(aminoadipyl)-L-cysteinyl-D-allo-isoleucine + AMP + diphosphate
L-2-aminoadipate + L-cysteine + L-isoleucine + ATP
L-delta-(aminoadipyl)-L-cysteinyl-D-isoleucine + AMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
L-2-aminoadipate + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
L-2-aminoadipate + L-homocysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-homocysteinyl-D-valine + AMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
L-2-aminoadipate + vinylglycine + L-valine + ATP
L-delta-(aminoadipyl)-L-vinylglycinyl-D-valine + AMP + diphosphate
L-glutamate + L-cysteine + L-valine + ATP
L-glutamyl-L-cysteinyl-D-valine + AMP + diphosphate
-
Substrates: -
Products: -
Products: -
?
S-carboxymethylcysteine + L-cysteine + L-valine + ATP
L-S-carboxymethylcysteinyl-L-cysteinyl-D-valine + AMP + diphosphate
3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O
3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
Substrates: -
Products: -
Products: -
?
3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O
3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
-
Substrates: -
Products: -
Products: -
?
3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O
3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
Substrates: -
Products: -
Products: -
?
ATP + (R)-4-phosphopantoate + beta-alanine
AMP + diphosphate + (R)-4'-phosphopantothenate
Substrates: the enzyme is involved in coenzyme A biosynthesis in the archaea
Products: -
Products: -
?
ATP + (R)-4-phosphopantoate + beta-alanine
AMP + diphosphate + (R)-4'-phosphopantothenate
Substrates: strict preference for ATP. Among several amine substrates, activity is detected with beta-alanine, but not with gamma-aminobutyrate, glycine nor aspartate
Products: -
Products: -
?
L-2-aminoadipate + allylglycine + L-valine + ATP
L-delta-(aminoadipyl)-L-allylglycinyl-D-valine + AMP + diphosphate
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Substrates: -
Products: -
Products: -
?
L-2-aminoadipate + allylglycine + L-valine + ATP
L-delta-(aminoadipyl)-L-allylglycinyl-D-valine + AMP + diphosphate
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Substrates: -
Products: -
Products: -
?
L-2-aminoadipate + L-cysteine + L-allo-isoleucine + ATP
L-delta-(aminoadipyl)-L-cysteinyl-D-allo-isoleucine + AMP + diphosphate
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Substrates: -
Products: -
Products: -
?
L-2-aminoadipate + L-cysteine + L-allo-isoleucine + ATP
L-delta-(aminoadipyl)-L-cysteinyl-D-allo-isoleucine + AMP + diphosphate
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Substrates: -
Products: -
Products: -
?
L-2-aminoadipate + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
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Substrates: -
Products: -
Products: -
?
L-2-aminoadipate + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
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Substrates: -
Products: -
Products: -
?
L-2-aminoadipate + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
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Substrates: -
Products: -
Products: -
?
L-2-aminoadipate + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
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Substrates: -
Products: -
Products: -
?
L-2-aminoadipate + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
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Substrates: -
Products: -
Products: -
?
L-2-aminoadipate + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
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Substrates: -
Products: -
Products: -
?
L-2-aminoadipate + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
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Substrates: -
Products: -
Products: -
?
L-2-aminoadipate + L-cysteine + L-valine + ATP
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + AMP + diphosphate
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Substrates: -
Products: -
Products: -
ir
L-2-aminoadipate + vinylglycine + L-valine + ATP
L-delta-(aminoadipyl)-L-vinylglycinyl-D-valine + AMP + diphosphate
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Substrates: -
Products: -
Products: -
?
L-2-aminoadipate + vinylglycine + L-valine + ATP
L-delta-(aminoadipyl)-L-vinylglycinyl-D-valine + AMP + diphosphate
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Substrates: -
Products: -
Products: -
?
S-carboxymethylcysteine + L-cysteine + L-valine + ATP
L-S-carboxymethylcysteinyl-L-cysteinyl-D-valine + AMP + diphosphate
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Substrates: -
Products: -
Products: -
?
S-carboxymethylcysteine + L-cysteine + L-valine + ATP
L-S-carboxymethylcysteinyl-L-cysteinyl-D-valine + AMP + diphosphate
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Substrates: -
Products: -
Products: -
?
additional information
?
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Substrates: ACVSs are multifunctional enzymes that activate amino acids as aminoacyladenylates, forming a mixed anhydride with the a-phosphate group of ATP and releasing pyrophosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: pure Streptomyces lactamdurans ACVS is able to activate alpha-aminoadipic acid or its lactam 6-oxopiperideine-2-carboxylic acid, a compound that is easily converted to alpha-aminoadipic acid, but is unable to use piperideine-6-carboxylate or pipecolic acid as substrates, enzyme is also able to use L-cystathionine with the same efficiency as L-cysteine
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
3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O
3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
alpha-aminoadipic acid + L-valine + L-lysine + ?
L-delta-alpha-aminoadipyl-L-cysteinyl-D-valine + ?
-
Substrates: enzyme is a nonribosomal peptide synthetase (NRPS) able to form ribosome-independent peptide bonds
Products: ACV
Products: ACV
?
ATP + (R)-4-phosphopantoate + beta-alanine
AMP + diphosphate + (R)-4'-phosphopantothenate
Substrates: the enzyme is involved in coenzyme A biosynthesis in the archaea
Products: -
Products: -
?
3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O
3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
Substrates: -
Products: -
Products: -
?
3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O
3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
-
Substrates: -
Products: -
Products: -
?
3 ATP + L-2-aminohexanedioate + L-cysteine + L-valine + H2O
3 AMP + 3 diphosphate + N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: ACVSs are multifunctional enzymes that activate amino acids as aminoacyladenylates, forming a mixed anhydride with the a-phosphate group of ATP and releasing pyrophosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: pure Streptomyces lactamdurans ACVS is able to activate alpha-aminoadipic acid or its lactam 6-oxopiperideine-2-carboxylic acid, a compound that is easily converted to alpha-aminoadipic acid, but is unable to use piperideine-6-carboxylate or pipecolic acid as substrates, enzyme is also able to use L-cystathionine with the same efficiency as L-cysteine
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
the non-ribosomal multidomain ACV synthetase requires ATP and Mg2+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
the non-ribosomal multidomain ACV synthetase requires ATP and Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-glucose
-
crude extract is inhibited due to deprivation of ATP via sugar metabolism
phosphate
-
ACVS activity decreases 30% in the presence of 100 mM phosphate, being also affected by AMP and pyrophosphate, products of ATP hydrolysis
5,5'-dithiobis-2-nitrobenzoate
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the major effect on ACVS activity is exerted by thiol-blocking agents, which almost completely inhibited the activity at 1 mM concentration, confirming the importance of thiol groups in ACVS activity
iodoacetamide
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the major effect on ACVS activity is exerted by thiol-blocking agents, which almost completely inhibited the activity at 1 mM concentration, confirming the importance of thiol groups in ACVS activity
N-ethylmaleimide
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the major effect on ACVS activity is exerted by thiol-blocking agents, which almost completely inhibited the activity at 1 mM concentration, confirming the importance of thiol groups in ACVS activity
additional information
PenV i.e. Pc22g22150 protein, located in the vacuolar membrane, affects drastically the biosynthesis of the ACV tripeptide and the beta-lactam pathway of Penicillium chrysogenum, overview
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additional information
-
PenV i.e. Pc22g22150 protein, located in the vacuolar membrane, affects drastically the biosynthesis of the ACV tripeptide and the beta-lactam pathway of Penicillium chrysogenum, overview
-
additional information
feedback inhibition by CoA/acetyl-CoA and product inhibition by 4'-phosphopantothenate are not observed
-
additional information
-
feedback inhibition by CoA/acetyl-CoA and product inhibition by 4'-phosphopantothenate are not observed
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65 - 95
activity continues to increase with temperature elevation from 65Ā°C up to 95Ā°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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brenda
a low penicillin production strain, gene pcbAB, the strain contains a single copy of the penicillin gene cluster
UniProt
brenda
a low penicillin production strain, gene pcbAB
UniProt
brenda
a low penicillin production strain, gene pcbAB, the strain contains a single copy of the penicillin gene cluster
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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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
physiological function
additional information
malfunction
RNAi-mediated silencing of penV gene, encoding protein Pc22g22150, UniProt-ID B6HTR9, provokes a drastic reduction of the production of the delta-(L-alpha-aminoadipyl-L-cysteinyl-D-valine) and isopenicillin N intermediates and the final product of the pathway
malfunction
-
RNAi-mediated silencing of penV gene, encoding protein Pc22g22150, UniProt-ID B6HTR9, provokes a drastic reduction of the production of the delta-(L-alpha-aminoadipyl-L-cysteinyl-D-valine) and isopenicillin N intermediates and the final product of the pathway
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physiological function
the enzyme catalyzes the non-ribosomal activation and condensation of the three constituent amino acids to form the tripeptide N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine, i.e. ACV
physiological function
-
after heat shock, ACVS is singificantly upregulated. Phosphopantetheinyl transferase is coregulated with ACVS, confirming its role in activating ACVS. All components for L-alpha-aminoadipic acid synthesis are present and transcriptionally active in Folsomia candida
physiological function
-
the enzyme catalyzes the non-ribosomal activation and condensation of the three constituent amino acids to form the tripeptide N-[L-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine, i.e. ACV
-
additional information
the ACVS is able to catalyse multiple activities including substrate amino acids adenylation, peptide-bond formation, epimerization and tripeptide release by an integrated thioesterase, since it contains three different modules each of approximately 1000 amino acids. The enzyme contains at least ten catalytic domains. The C-terminal region of ACVS bears the epimerase and the thioesterase domains and may be involved in the epimerization of LLL-ACV to LLD-ACV and in the hydrolysis of the thioester bond. Residues E3371, H3373, R3375 and E3376 belong to the epimerase active centre. Different fragments included in the C-terminal region of the enzyme control thioester hydrolysis. Role of the EGHGRE motif present in the epimerase domain of ACVS, the epimerization domain located in the third module (activating L-valine) contains seven partially conserved motifs E1 to E7, overview. The EGHGRE motif containing residues E3371, H3373, R3375 and E3376 is crucial for the activity of the ACVS, involvement of the GWSFG motif in the ACVS activity
additional information
-
the ACVS is able to catalyse multiple activities including substrate amino acids adenylation, peptide-bond formation, epimerization and tripeptide release by an integrated thioesterase, since it contains three different modules each of approximately 1000 amino acids. The enzyme contains at least ten catalytic domains. The C-terminal region of ACVS bears the epimerase and the thioesterase domains and may be involved in the epimerization of LLL-ACV to LLD-ACV and in the hydrolysis of the thioester bond. Residues E3371, H3373, R3375 and E3376 belong to the epimerase active centre. Different fragments included in the C-terminal region of the enzyme control thioester hydrolysis. Role of the EGHGRE motif present in the epimerase domain of ACVS, the epimerization domain located in the third module (activating L-valine) contains seven partially conserved motifs E1 to E7, overview. The EGHGRE motif containing residues E3371, H3373, R3375 and E3376 is crucial for the activity of the ACVS, involvement of the GWSFG motif in the ACVS activity
additional information
-
the ACVS is able to catalyse multiple activities including substrate amino acids adenylation, peptide-bond formation, epimerization and tripeptide release by an integrated thioesterase, since it contains three different modules each of approximately 1000 amino acids. The enzyme contains at least ten catalytic domains. The C-terminal region of ACVS bears the epimerase and the thioesterase domains and may be involved in the epimerization of LLL-ACV to LLD-ACV and in the hydrolysis of the thioester bond. Residues E3371, H3373, R3375 and E3376 belong to the epimerase active centre. Different fragments included in the C-terminal region of the enzyme control thioester hydrolysis. Role of the EGHGRE motif present in the epimerase domain of ACVS, the epimerization domain located in the third module (activating L-valine) contains seven partially conserved motifs E1 to E7, overview. The EGHGRE motif containing residues E3371, H3373, R3375 and E3376 is crucial for the activity of the ACVS, involvement of the GWSFG motif in the ACVS activity
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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). ACVA_ACRCH
3712
0
414775
Swiss-Prot
other Location (Reliability: 1)
ACVA_EMENI
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
3770
0
422502
Swiss-Prot
other Location (Reliability: 1)
ACVA_PENCH
3746
0
421076
Swiss-Prot
other Location (Reliability: 3)
ACVA_PENRW
Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255)
3746
0
421076
Swiss-Prot
other Location (Reliability: 3)
B8MM62_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
3939
0
437436
TrEMBL
other Location (Reliability: 1)
A0A077NVQ2_XENBV
1857
0
204376
TrEMBL
-
E3FPD1_STIAD
Stigmatella aurantiaca (strain DW4/3-1)
3678
0
405856
TrEMBL
-
Q3M5N6_TRIV2
Trichormus variabilis (strain ATCC 29413 / PCC 7937)
2033
0
227558
TrEMBL
-
B8M109_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
5091
0
566090
TrEMBL
other Location (Reliability: 2)
A0A077N8A5_XENBV
1857
0
204341
TrEMBL
-
B7PXZ1_IXOSC
342
0
38333
TrEMBL
other Location (Reliability: 2)
I2C685_BACAY
Bacillus amyloliquefaciens (strain Y2)
2568
0
289279
TrEMBL
-
I2C683_BACAY
Bacillus amyloliquefaciens (strain Y2)
1202
0
135342
TrEMBL
-
Q3MCQ0_TRIV2
Trichormus variabilis (strain ATCC 29413 / PCC 7937)
3498
0
392563
TrEMBL
-
A0A0N1G388_9ACTN
1882
0
203993
TrEMBL
-
B7P268_IXOSC
1561
0
169086
TrEMBL
other Location (Reliability: 1)
A0A0N1G197_9ACTN
821
0
86710
TrEMBL
-
I2CAP2_BACAY
Bacillus amyloliquefaciens (strain Y2)
875
0
100001
TrEMBL
-
A0A077PM67_XENBV
1830
0
201154
TrEMBL
-
A0A0F4YTD2_TALEM
5095
0
567789
TrEMBL
other Location (Reliability: 3)
B8M4E7_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
5650
0
625696
TrEMBL
other Location (Reliability: 1)
I2C5E7_BACAY
Bacillus amyloliquefaciens (strain Y2)
1877
0
206163
TrEMBL
-
B8MC36_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
2930
0
325964
TrEMBL
other Location (Reliability: 3)