KEGG   ENZYME: 6.3.2.49
Entry
EC 6.3.2.49                 Enzyme                                 
Name
L-alanine---L-anticapsin ligase;
BacD;
alanine-anticapsin ligase;
L-Ala-L-anticapsin ligase;
ywfE (gene name)
Class
Ligases;
Forming carbon-nitrogen bonds;
Acid-D-amino-acid ligases (peptide synthases)
Sysname
L-alanine:L-anticapsin ligase (ADP-forming)
Reaction(IUBMB)
ATP + L-alanine + L-anticapsin = ADP + phosphate + bacilysin [RN:R11064]
Reaction(KEGG)
R11064
Substrate
ATP [CPD:C00002];
L-alanine [CPD:C00041];
L-anticapsin [CPD:C20941]
Product
ADP [CPD:C00008];
phosphate [CPD:C00009];
bacilysin [CPD:C20942]
Comment
The enzyme, characterized from the bacterium Bacillus subtilis, is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. The enzyme requires Mg2+ or Mn2+ for activity, and has a broad substrate specificity in vitro [1].
History
EC 6.3.2.49 created 2006 as EC 6.3.2.28, transferred 2015 to EC 6.3.2.49
Pathway
ec00998  Biosynthesis of various antibiotics
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K13037  L-alanine-L-anticapsin ligase
Genes
BSUBSU37710(bacD)
BSRI33_3919(bacD)
BSLA7A1_0190
BSHBSU6051_37710(bacD)
BSYI653_18500
BSUTBSUB_04007(bacD)
BSULBSUA_04007(bacD)
BSUSQ433_20770
BSOBSNT_10429(ywfE)
BSNBSn5_09845
BSQB657_37710(bacD)
BSXC663_3676(bacD)
BSPU712_19005
BSSBSUW23_18625(bacD)
BSTGYO_4157(bacD)
BAYRBAM_034900
BAQBACAU_3519(bacD)
BYABANAU_3672(bacD)
BAMPB938_17910(bacD)
BQYMUS_4149(bacD)
BAMLBAM5036_3420(bacD)
BAMARBAU_3628(bacD)
BAMNBASU_3404(bacD)
BAMBBAPNAU_3686(bacD)
BAMTAJ82_19695
BAMYV529_37620(bacD)
BMPNG74_03665(bacD_2)
BAOBAMF_3604(bacD)
BAZBAMTA208_19085(bacD)
BQLLL3_03915(bacD)
BXHBAXH7_03907(bacD)
BAMIKSO_001610
BAMCU471_36350
BAMFU722_18645
BSIACWD84_01675
BVMB9C48_17860
BHTDIC78_12120
BMOJHC660_36790(bacD)
BTEQG4P54_19445(bacD)
BIQAN935_19100
BPUBPUM_3423
BPUMBW16_18175
BPUSUP12_17620
BJSMY9_3862
BACWQR42_17175
BACPSB24_11245
BACBOY17_01115
BACYQF06_17295
BACLBS34A_40890(bacD)
BALMBsLM_3801
BALTCFN77_18080
BACSAUL54_12245
BSAFBSL056_18720
BITBIS30_08570
BGIBGM20_13115
BMURABE28_019130
PALRHGI30_05295
SSPBCP982_01625
 » show all
Reference
1  [PMID:16030213]
  Authors
Tabata K, Ikeda H, Hashimoto S
  Title
ywfE in Bacillus subtilis codes for a novel enzyme, L-amino acid ligase.
  Journal
J Bacteriol 187:5195-202 (2005)
DOI:10.1128/JB.187.15.5195-5202.2005
  Sequence
[bsu:BSU37710]
Reference
2  [PMID:22298000]
  Authors
Tsuda T, Suzuki T, Kojima S
  Title
Crystallization and preliminary X-ray diffraction analysis of Bacillus subtilis YwfE, an L-amino-acid ligase.
  Journal
Acta Crystallogr Sect F Struct Biol Cryst Commun 68:203-6 (2012)
DOI:10.1107/S174430911105425X
Reference
3  [PMID:22407814]
  Authors
Shomura Y, Hinokuchi E, Ikeda H, Senoo A, Takahashi Y, Saito J, Komori H, Shibata N, Yonetani Y, Higuchi Y
  Title
Structural and enzymatic characterization of BacD, an L-amino acid dipeptide ligase from Bacillus subtilis.
  Journal
Protein Sci 21:707-16 (2012)
DOI:10.1002/pro.2058
  Sequence
[bsu:BSU37710]
Reference
4  [PMID:23317005]
  Authors
Parker JB, Walsh CT
  Title
Action and timing of BacC and BacD in the late stages of biosynthesis of the dipeptide antibiotic bacilysin.
  Journal
Biochemistry 52:889-901 (2013)
DOI:10.1021/bi3016229
Other DBs
ExplorEnz - The Enzyme Database: 6.3.2.49
IUBMB Enzyme Nomenclature: 6.3.2.49
ExPASy - ENZYME nomenclature database: 6.3.2.49
BRENDA, the Enzyme Database: 6.3.2.49

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