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Enzyme Nomenclature
Information on EC 3.5.1.125 - N2-acetyl-L-2,4-diaminobutanoate deacetylase
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3.5.1.125 N2-acetyl-L-2,4-diaminobutanoate deacetylaseIUBMB Comments
The enzyme, found in bacteria, has no activity with (2S)-4-acetamido-2-aminobutanoate (cf. EC 3.5.4.44, ectoine hydrolase).
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The enzyme appears in viruses and cellular organisms
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
doeB
Helo_3664
N-alpha-acetyl-L-2,4-diaminobutyric acid deacetylase
doeB
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2S)-2-acetamido-4-aminobutanoate + H2O = L-2,4-diaminobutanoate + acetate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
N2-acetyl-L-2,4-diaminobutanoate amidohydrolase
The enzyme, found in bacteria, has no activity with (2S)-4-acetamido-2-aminobutanoate (cf. EC 3.5.4.44, ectoine hydrolase).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N2-acetyl-L-2,4-diaminobutanoate + H2O
L-2,4-diaminobutanoate + acetate
-
-
-
?
N2-acetyl-L-2,4-diaminobutanoate + H2O
L-2,4-diaminobutanoate + acetate
-
-
-
?
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
the degradation of ectoine proceeds via hydrolysis of ectoine by DoeA to Nalpha-acetyl-L-2,4-diaminobutanoate, followed by deacetylation to diaminobutanoate by DoeB and a transaminase reaction by DoeD leading to aspartate-semialdehyde. Deletion of doeB result in a mutant that cannot utilize ectoine as carbon and nitrogen source. Nalpha-acetyl-L-2,4-diaminobutanoate accumulates as the predominant amino-reactive solute in the mutant while no Nalpha-acetyl-L-2,4-diaminobutanoate is detectable in the wild type
physiological function
-
the degradation of ectoine proceeds via hydrolysis of ectoine by DoeA to Nalpha-acetyl-L-2,4-diaminobutanoate, followed by deacetylation to diaminobutanoate by DoeB and a transaminase reaction by DoeD leading to aspartate-semialdehyde. Deletion of doeB result in a mutant that cannot utilize ectoine as carbon and nitrogen source. Nalpha-acetyl-L-2,4-diaminobutanoate accumulates as the predominant amino-reactive solute in the mutant while no Nalpha-acetyl-L-2,4-diaminobutanoate is detectable in the wild type
-
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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). DOEB_HALED
Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9)
342
0
36586
Swiss-Prot
-
A0A6J4ZXZ0_9BURK
342
0
36516
TrEMBL
-
B1G1E2_PARG4
Paraburkholderia graminis (strain ATCC 700544 / DSM 17151 / LMG 18924 / NCIMB 13744 / C4D1M)
341
0
37045
TrEMBL
-
A0A6J5KC09_9BURK
211
0
22000
TrEMBL
-
A0A6J5K2N9_9BURK
343
0
37192
TrEMBL
-
A0A6J5K0B9_9BURK
342
0
36517
TrEMBL
-
A0A6L5BTC5_9PSED
338
0
37418
TrEMBL
-
A0A6J5ASQ5_9BURK
343
0
37134
TrEMBL
-
A0A543Q000_ACITH
300
0
33789
TrEMBL
-
A0A644Y128_9ZZZZ
314
0
34270
TrEMBL
other Location (Reliability: 1)
B1G109_PARG4
Paraburkholderia graminis (strain ATCC 700544 / DSM 17151 / LMG 18924 / NCIMB 13744 / C4D1M)
340
0
36245
TrEMBL
-
A0A346BJQ9_9BURK
330
0
35466
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schwibbert, K.; Marin-Sanguino, A.; Bagyan, I.; Heidrich, G.; Lentzen, G.; Seitz, H.; Rampp, M.; Schuster, S.C.; Klenk, H.P.; Pfeiffer, F.; Oesterhelt, D.; Kunte, H.J.
A blueprint of ectoine metabolism from the genome of the industrial producer Halomonas elongata DSM 2581 T
Environ. Microbiol.
13
1973-1994
2011
Halomonas elongata (E1V7W0), Halomonas elongata DSM 2581 (E1V7W0)
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