KEGG   ENZYME: 6.3.2.54Help
Entry
EC 6.3.2.54                 Enzyme                                 

Name
L-2,3-diaminopropanoate---citrate ligase;
sbnE (gene name);
2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate synthtase
Class
Ligases;
Forming carbon-nitrogen bonds;
Acid-D-amino-acid ligases (peptide synthases)
BRITE hierarchy
Sysname
L-2,3-diaminopropanoate:citrate ligase (2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate-forming)
Reaction(IUBMB)
ATP + L-2,3-diaminopropanoate + citrate = AMP + diphosphate + 2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate [RN:R12308]
Reaction(KEGG)
Substrate
ATP [CPD:C00002];
L-2,3-diaminopropanoate [CPD:C03401];
citrate [CPD:C00158]
Product
AMP [CPD:C00020];
diphosphate [CPD:C00013];
2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate [CPD:C22072]
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 A nonribosomal peptide synthase-independent synthases (NIS). Type A NIS enzymes are responsible for the formation of amide or ester bonds between polyamines or amino alcohols and a prochiral carboxyl group of citrate. The enzyme forms a citrate adenylate intermediate prior to ligation.
History
EC 6.3.2.54 created 2019
Pathway
ec00997  Biosynthesis of various secondary metabolites - part 3
ec01100  Metabolic pathways
Orthology
K23372  L-2,3-diaminopropanoate---citrate ligase
Genes
RSL: RPSI07_mp0382
RSN: RSPO_m01407
RSM: CMR15_mp10434
RSE: F504_3903(sbnE)
RSY: RSUY_34890(iucA)
RPU: CDC45_19735
CNC: CNE_2c14870
CUH: BJN34_08305
BPLA: bpln_2g05050
NLC: EBAPG3_006470
SAU: SA0116(sbnE)
SAV: SAV0120
SAW: SAHV_0119
SAM: MW0093(sbnE)
SAS: SAS0094
SAR: SAR0123
SAC: SACOL0104
SAE: NWMN_0064(sbnE)
SAD: SAAV_0088
SUU: M013TW_0110(sbnE)
SUE: SAOV_0067
SUJ: SAA6159_00103(sbnE)
SUK: SAA6008_00098(sbnE)
SUC: ECTR2_76
SUZ: MS7_0112
SUW: SATW20_01320(sbnE)
SUG: SAPIG0132
SUF: SARLGA251_00950(sbnE)
SAUA: SAAG_00604
SAUS: SA40_0087(sbnE)
SAUU: SA957_0102(sbnE)
SAUG: SA268_0099(sbnE)
SAUZ: SAZ172_0131(sbnE)
SAUF: X998_0099
SAB: SAB0059
SUY: SA2981_0121(sbnE)
SAUB: C248_0108
SAUM: BN843_1220
SAUC: CA347_131
SAUR: SABB_01720(sbnE)
SAUI: AZ30_00625
SAUD: CH52_05120
SAMS: NI36_00520
SDT: SPSE_2120
SHU: SHYC_00375(sbnE)
SSCH: LH95_00375
SSCZ: RN70_00595
SAGQ: EP23_09750
PPOL: X809_04485
 » show all
Taxonomy
Reference
1  [PMID:14688077]
  Authors
Dale SE, Doherty-Kirby A, Lajoie G, Heinrichs DE
  Title
Role of siderophore biosynthesis in virulence of Staphylococcus aureus: identification and characterization of genes involved in production of a siderophore.
  Journal
Infect Immun 72:29-37 (2004)
DOI:10.1128/IAI.72.1.29-37.2004
  Sequence
[sam:MW0093]
Reference
2  [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: 6.3.2.54
IUBMB Enzyme Nomenclature: 6.3.2.54
ExPASy - ENZYME nomenclature database: 6.3.2.54
BRENDA, the Enzyme Database: 6.3.2.54

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