KEGG   ENZYME: 6.3.2.55Help
Entry
EC 6.3.2.55                 Enzyme                                 

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 secondary metabolites - part 3
ec01100  Metabolic pathways
Orthology
K23374  2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate synthase
Genes
BUL: BW21_4936
BUD: AQ610_28500
SAU: SA0117(sbnF)
SAV: SAV0121
SAW: SAHV_0120
SAH: SaurJH1_0112
SAJ: SaurJH9_0108
SAM: MW0094(sbnF)
SAS: SAS0095
SAR: SAR0124
SAC: SACOL0105
SAE: NWMN_0065(sbnF)
SAD: SAAV_0089
SUU: M013TW_0111(sbnF)
SUE: SAOV_0068
SUC: ECTR2_77
SUZ: MS7_0113
SUW: SATW20_01330(sbnF)
SUG: SAPIG0133
SUF: SARLGA251_00960(sbnF)
SAUA: SAAG_00605
SAUS: SA40_0088(sbnF)
SAUU: SA957_0103(sbnF)
SAUG: SA268_0100(sbnF)
SAUZ: SAZ172_0132(sbnF)
SAUF: X998_0100
SAB: SAB0060
SUY: SA2981_0122(sbnF)
SAUB: C248_0109
SAUM: BN843_1230
SAUC: CA347_132
SAUR: SABB_03469
SAUI: AZ30_00630
SAUD: CH52_05115
SAMS: NI36_00525
SDT: SPSE_2119
SHU: SHYC_00380(sbnF)
SSCH: LH95_00380
SSCZ: RN70_00600
SAGQ: EP23_09745
 » show all
Taxonomy
Reference
1  [PMID:19775248]
  Authors
Cheung J, Beasley FC, Liu S, Lajoie GA, Heinrichs DE
  Title
Molecular characterization of staphyloferrin B biosynthesis in Staphylococcus aureus.
  Journal
Mol Microbiol 74:594-608 (2009)
DOI:10.1111/j.1365-2958.2009.06880.x
Other DBs
ExplorEnz - The Enzyme Database: 6.3.2.55
IUBMB Enzyme Nomenclature: 6.3.2.55
ExPASy - ENZYME nomenclature database: 6.3.2.55
BRENDA, the Enzyme Database: 6.3.2.55

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