KEGG   ENZYME: 6.3.2.46
Entry
EC 6.3.2.46                 Enzyme                                 
Name
fumarate---(S)-2,3-diaminopropanoate ligase;
DdaG;
fumarate:(S)-2,3-diaminopropanoate ligase (AMP-forming)
Class
Ligases;
Forming carbon-nitrogen bonds;
Acid-D-amino-acid ligases (peptide synthases)
Sysname
fumarate:L-2,3-diaminopropanoate ligase (AMP-forming)
Reaction(IUBMB)
ATP + fumarate + L-2,3-diaminopropanoate = AMP + diphosphate + N3-fumaroyl-L-2,3-diaminopropanoate [RN:R10940]
Reaction(KEGG)
R10940
Substrate
ATP [CPD:C00002];
fumarate [CPD:C00122];
L-2,3-diaminopropanoate [CPD:C03401]
Product
AMP [CPD:C00020];
diphosphate [CPD:C00013];
N3-fumaroyl-L-2,3-diaminopropanoate [CPD:C20961]
Comment
The enzyme, characterized from the bacterium Enterobacter agglomerans, is involved in biosynthesis of dapdiamide tripeptide antibiotics, a family of fumaramoyl- and epoxysuccinamoyl-peptides named for the presence of an L-2,3-diaminopropanoate (DAP) moiety and two amide linkages in their scaffold.
History
EC 6.3.2.46 created 2015
Pathway
ec00998  Biosynthesis of various antibiotics
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K22113  fumarate---(S)-2,3-diaminopropanoate ligase
Genes
SPESpro_0345
SPLYQ5A_016900
PVAPvag_pPag20164
PAGCBEE12_22715
PMAMKSS90_08440
PALOE6C60_3194
PCELHUB94_19670
PALRHGI30_17415
CCHLFPL14_15945
SGDELQ87_36080
Reference
1  [PMID:19807062]
  Authors
Hollenhorst MA, Clardy J, Walsh CT
  Title
The ATP-dependent amide ligases DdaG and DdaF assemble the fumaramoyl-dipeptide scaffold of the dapdiamide antibiotics.
  Journal
Biochemistry 48:10467-72 (2009)
DOI:10.1021/bi9013165
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 6.3.2.46
IUBMB Enzyme Nomenclature: 6.3.2.46
ExPASy - ENZYME nomenclature database: 6.3.2.46
BRENDA, the Enzyme Database: 6.3.2.46
LinkDB

DBGET integrated database retrieval system