KEGG ENZYME: 6.3.2.49

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

BSU:	BSU37710(bacD)

BSR:	I33_3919(bacD)

BSL:

A7A1_0190

BSH:	BSU6051_37710(bacD)

BSY:	I653_18500

BSUT:

BSUB_04007(bacD)

BSUL:

BSUA_04007(bacD)

BSUS:

Q433_20770

BSO:	BSNT_10429(ywfE)

BSN:	BSn5_09845

BSQ:	B657_37710(bacD)

BSX:	C663_3676(bacD)

BSP:	U712_19005

BSS:	BSUW23_18625(bacD)

BST:	GYO_4157(bacD)

BIT:	BIS30_08570

BAY:	RBAM_034900

BAQ:	BACAU_3519(bacD)

BYA:	BANAU_3672(bacD)

BAMP:

B938_17910(bacD)

BQY:	MUS_4149(bacD)

BAML:

BAM5036_3420(bacD)

BAMA:

RBAU_3628(bacD)

BAMN:

BASU_3404(bacD)

BAMB:

BAPNAU_3686(bacD)

BAMT:

AJ82_19695

BAMY:

V529_37620(bacD)

BMP:	NG74_03665(bacD_2)

BAO:	BAMF_3604(bacD)

BAZ:	BAMTA208_19085(bacD)

BQL:	LL3_03915(bacD)

BXH:	BAXH7_03907(bacD)

BAMI:

KSO_001610

BAMC:

U471_36350

BAMF:

U722_18645

BSIA:

CWD84_01675

BVM:	B9C48_17860

BHT:	DIC78_12120

BMOJ:

HC660_36790(bacD)

BTEQ:

G4P54_19445(bacD)

BIQ:	AN935_19100

BSTR:

QI003_22360(bacD)

BPU:

BPUM_3423

BPUM:

BW16_18175

BPUS:

UP12_17620

BALT:

CFN77_18080

BAER:

BAE_05980

BSAF:

BSL056_18720

BCAB:

EFK13_19415(bacD)

BRY:	M0696_19165(bacD)

BJS:

MY9_3862

BACW:

QR42_17175

BACP:

SB24_11245

BACB:

OY17_01115

BACY:

QF06_17295

BACL:

BS34A_40890(bacD)

BALM:

BsLM_3801

BACS:

AUL54_12245

BZH:	NF868_15810

BAEI:

RE735_02170

BGI:	BGM20_13115

BMUR:

ABE28_019130

PALR:

HGI30_05295

SSPB:

CP982_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

LinkDB

DBGET integrated database retrieval system