Entry
Name
2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate synthase;
sbnF (gene name)
Class
Ligases;
Forming carbon-nitrogen bonds;
Acid-D-amino-acid ligases (peptide synthases)
BRITE hierarchy
Sysname
2-[(2-aminoethylcarbamoyl)methyl]-2-hydroxybutanedioate:L-2,3-diaminopropanoate ligase {2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate-forming}
Reaction(IUBMB)
ATP + 2-[(2-aminoethylcarbamoyl)methyl]-2-hydroxybutanedioate + L-2,3-diaminopropanoate = AMP + diphosphate + 2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate [RN:
R12311 ]
Reaction(KEGG)
Substrate
ATP [CPD:
C00002 ];
2-[(2-aminoethylcarbamoyl)methyl]-2-hydroxybutanedioate [CPD:
C22073 ];
L-2,3-diaminopropanoate [CPD:
C03401 ]
Product
AMP [CPD:
C00020 ];
diphosphate [CPD:
C00013 ];
2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate [CPD:
C22074 ]
Comment
Requires Mg2+. The enzyme, characterized from the bacterium Staphylococcus aureus, is involved in the biosynthesis of the siderophore staphyloferrin B. It belongs to a class of siderophore synthases known as type C nonribosomal peptide synthase-independent synthases (NIS). Type C NIS enzymes recognize esterified or amidated derivatives of carboxylic acids. The enzyme likely forms a 2-[(2-aminoethylcarbamoyl)methyl]-2-hydroxybutanedioate adenylate intermediate prior to ligation.
History
EC 6.3.2.55 created 2019
Pathway
ec00997 Biosynthesis of various other secondary metabolites
ec01110 Biosynthesis of secondary metabolites
Orthology
K23374 2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate synthase
Genes
MIWA : SS37A_35500 SS37A_39100
PCAL : BV455_03919(iucC_1)
SUF : SARLGA251_00960(sbnF)
SDP : NCTC12225_02336(iucC_3)
SSH : NCTC13712_00074(iucC_2)
ANX : ACH33_02535 ACH33_02540
SACA : FFV09_03640 FFV09_03645
TUM : CBW65_11375 CBW65_11410
» show all
Taxonomy
Reference
Authors
Cheung J, Beasley FC, Liu S, Lajoie GA, Heinrichs DE
Title
Molecular characterization of staphyloferrin B biosynthesis in Staphylococcus aureus.
Journal
Other DBs
ExplorEnz - The Enzyme Database: 6.3.2.55
ExPASy - ENZYME nomenclature database: 6.3.2.55