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besA

Gene
besA
Protein
L-propargylglycine--L-glutamate ligase
Organism
Streptomyces cattleya (strain ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057)
Length
482 amino acids
Function
Involved in the biosynthesis of terminal alkyne-containing amino acids produced as antibiotics by S.cattleya. Catalyzes the ATP-dependent ligation of L-propargylglycine to L-glutamate to form the dipeptide L-gamma-glutamyl-L-propargylglycine. Is selective for L-propargylglycine over norvaline, allylglycine and the standard proteinogenic amino acids, except L-cysteine which can be used as a substrate to a lesser extent.
Mass
52.271 kDa
Sequence
MYGAGVVTRMNEAERFHMTDPGSTKILIYAFNYADRMLEEVPYLRYSAERSLCFLGDLRDPGTRLVVITSEAVDPATLDYHLRDVFRFDEPALADVRRRLTLLTPASRAARPLDSLVLEDEALVETLRRAVAERPAGTIVDFSASPATDELGRRTGATPEEGDHAFVARWGSKSGGKEICLRAGVAVPGGTSEVLRSEAEVVEAIHRLSCGTAAARRAMVKLDAITWAASIGNVLIDRDKLRHTGDLVGSAEVIRLPAEEFRRELAEQGAIVEEFLEEITDSPSGLGHIERDGTVRVVACHDQVLSGGQYWGCRFPADERWRPEITDAVRRTGEVLSGLGHRGAFGVDFVVAGERGLLAVEINLRKVGPSHVVRYAEALVGARVGADGMLRGADGRPVYYTHGRLLEPETLGKLNPRTAVERLRAEGLLYRHDTGEGVALHVLGALNACGFVELTALARSPEAADGYSRAAQALLTGPYPSA

Gene
besA
Protein
Ferri-bacillibactin esterase BesA
Organism
Bacillus subtilis (strain 168)
Length
289 amino acids
Function
Catalyzes the hydrolysis of the trilactone cycle of ferri-bacillibactin (ferri-BB) complex, leading to the formation of bacillibactin monomers and to cytosolic iron release, thus making iron available for metabolic use. Can also hydrolyze bacillibactin (BB), however the catalytic efficiency for ferri-BB hydrolysis is much higher than for BB.
Similarity
Belongs to the esterase D family.
Mass
32.439 kDa
Sequence
MKEQTTDRTNGGTSNAFTIPGTEVRMMSSRNENRTYHIFISKPSTPPPPAGYPVIYLLDANSVFGTMTEAVRIQGRRPEKTGVIPAVIVGIGYETAEPFSSARHRDFTMPTAQSKLPERPDGREWPEHGGAEGFFRFIEEDLKPEIERDYQIDKKRQTIFGHSLGGLFVLQVLLTKPDAFQTYIAGSPSIHWNKPFILKKTDHFVSLTKKNNQPINILLAAGELEQHHKSRMNDNARELYERLAVLSEQGIRAEFCEFSGEGHISVLPVLVSRALRFALHPDGPHLSMG