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Information on EC 2.6.1.111 - 3-aminobutanoyl-CoA transaminase
for references in articles please use BRENDA:EC2.6.1.111
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EC Tree 2 Transferases
2.6 Transferring nitrogenous groups
2.6.1 Transaminases
2.6.1.111 3-aminobutanoyl-CoA transaminase
IUBMB Comments
The enzyme, found in bacteria, is part of a L-lysine degradation pathway. The enzyme is also active with other β-amino compounds such as 3-amino-5-methylhexanoyl-CoA and 3-amino-3-phenylpropanoyl-CoA.
The expected taxonomic range for this enzyme is: Candidatus Cloacimonas acidaminovorans
showSynonyms
3-aminobutyryl-CoA aminotransferase, acyl-CoA beta-transaminase, KAT, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-aminobutyryl-CoA aminotransferase
acyl-CoA beta-transaminase
KAT
acyl-CoA beta-transaminase
-
-
-
-
KAT
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-aminobutanoyl-CoA + 2-oxoglutarate = acetoacetyl-CoA + L-glutamate
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
3-aminobutanoyl-CoA:2-oxoglutarate aminotransferase
The enzyme, found in bacteria, is part of a L-lysine degradation pathway. The enzyme is also active with other beta-amino compounds such as 3-amino-5-methylhexanoyl-CoA and 3-amino-3-phenylpropanoyl-CoA.
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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
S-[2-(acetylamino)ethyl] 3-amino-3-phenylpropanethioate + 2-oxoglutarate
S-[2-(acetylamino)ethyl] 3-oxo-3-phenylpropanethioate + L-glutamate
S-[2-(acetylamino)ethyl] 3-amino-5-methylhexanethioate + 2-oxoglutarate
S-[2-(acetylamino)ethyl] 3-oxo-5-methylhexanethioate + L-glutamate
S-[2-(acetylamino)ethyl] 3-aminobutanethioate + 2-oxoglutarate
S-[2-(acetylamino)ethyl] 3-oxobutanethioate + L-glutamate
(3S)-3-aminobutanoyl-CoA + 2-oxoglutarate
acetoacetyl-CoA + L-glutamate
Substrates: -
Products: -
Products: -
?
(3S)-3-aminobutanoyl-CoA + 2-oxoglutarate
acetoacetyl-CoA + L-glutamate
Substrates: -
Products: -
Products: -
?
(3S)-3-aminobutanoyl-CoA + pyruvate
acetoacetyl-CoA + L-alanine
Substrates: -
Products: -
Products: -
?
(3S)-3-aminobutanoyl-CoA + pyruvate
acetoacetyl-CoA + L-alanine
Substrates: -
Products: -
Products: -
?
S-[2-(acetylamino)ethyl] 3-amino-3-phenylpropanethioate + 2-oxoglutarate
S-[2-(acetylamino)ethyl] 3-oxo-3-phenylpropanethioate + L-glutamate
Substrates: i.e. beta-phenylalanine-S-(N-acetylcysteamine), N-acetylcysteamine can serve as a CoA mimic for Kat
Products: -
Products: -
?
S-[2-(acetylamino)ethyl] 3-amino-3-phenylpropanethioate + 2-oxoglutarate
S-[2-(acetylamino)ethyl] 3-oxo-3-phenylpropanethioate + L-glutamate
Substrates: i.e. beta-phenylalanine-S-(N-acetylcysteamine), N-acetylcysteamine can serve as a CoA mimic for Kat
Products: -
Products: -
?
S-[2-(acetylamino)ethyl] 3-amino-5-methylhexanethioate + 2-oxoglutarate
S-[2-(acetylamino)ethyl] 3-oxo-5-methylhexanethioate + L-glutamate
Substrates: i.e. beta-homoleucine-S-(N-acetylcysteamine), N-acetylcysteamine can serve as a CoA mimic for Kat
Products: -
Products: -
?
S-[2-(acetylamino)ethyl] 3-amino-5-methylhexanethioate + 2-oxoglutarate
S-[2-(acetylamino)ethyl] 3-oxo-5-methylhexanethioate + L-glutamate
Substrates: i.e. beta-homoleucine-S-(N-acetylcysteamine), N-acetylcysteamine can serve as a CoA mimic for Kat
Products: -
Products: -
?
S-[2-(acetylamino)ethyl] 3-aminobutanethioate + 2-oxoglutarate
S-[2-(acetylamino)ethyl] 3-oxobutanethioate + L-glutamate
Substrates: i.e. 3-aminobutanoyl-S-(N-acetylcysteamine), N-acetylcysteamine can serve as a CoA mimic for Kat
Products: -
Products: -
?
S-[2-(acetylamino)ethyl] 3-aminobutanethioate + 2-oxoglutarate
S-[2-(acetylamino)ethyl] 3-oxobutanethioate + L-glutamate
Substrates: i.e. 3-aminobutanoyl-S-(N-acetylcysteamine), N-acetylcysteamine can serve as a CoA mimic for Kat
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
(3S)-3-aminobutanoyl-CoA + 2-oxoglutarate
acetoacetyl-CoA + L-glutamate
Substrates: -
Products: -
Products: -
?
(3S)-3-aminobutanoyl-CoA + 2-oxoglutarate
acetoacetyl-CoA + L-glutamate
Substrates: -
Products: -
Products: -
?
(3S)-3-aminobutanoyl-CoA + pyruvate
acetoacetyl-CoA + L-alanine
Substrates: -
Products: -
Products: -
?
(3S)-3-aminobutanoyl-CoA + pyruvate
acetoacetyl-CoA + L-alanine
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
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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
physiological function
physiological function
gene product Kat may participate in an alternative pathway of lysine fermentation
physiological function
-
gene product Kat may participate in an alternative pathway of lysine fermentation
-
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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). KAT_CLOAI
Cloacimonas acidaminovorans (strain Evry)
414
0
46481
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Perret, A.; Lechaplais, C.; Tricot, S.; Perchat, N.; Vergne, C.; Pelle, C.; Bastard, K.; Kreimeyer, A.; Vallenet, D.; Zaparucha, A.; Weissenbach, J.; Salanoubat, M.
A novel acyl-CoA beta-transaminase characterized from a metagenome
PLoS ONE
6
e22918
2011
Candidatus Cloacimonas acidaminovorans (B0VH76), Candidatus Cloacimonas acidaminovorans Evry (B0VH76)
brenda
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Release 2026.1 (March 2026)
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