KEGG   ENZYME: 6.3.2.54
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)
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)
R12308
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 other secondary metabolites
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K23372  L-2,3-diaminopropanoate---citrate ligase
Genes
HSVHNO53_08390
RSORSp0421
RSLRPSI07_mp0382
RSNRSPO_m01407
RSMCMR15_mp10434
RSEF504_3903(sbnE)
RSYRSUY_34890(iucA)
RPUCDC45_19735
RSGJK151_14165
CNCCNE_2c14870
CUHBJN34_08305
RMERmet_1113
BPLAbpln_2g05050
NLCEBAPG3_006470
PAUUE8A73_020440
SBDATN00_04610
BBADK7T73_21440
PCALBV455_03920(iucA)
LGYT479_22390
SALEEPH95_16125
SAUSA0116(sbnE)
SAVSAV0120
SAWSAHV_0119
SAHSaurJH1_0111
SAJSaurJH9_0107
SAMMW0093(sbnE)
SASSAS0094
SARSAR0123
SACSACOL0104
SAXUSA300HOU_0131
SAASAUSA300_0122
SAOSAOUHSC_00079
SAENWMN_0064(sbnE)
SADSAAV_0088
SUUM013TW_0110(sbnE)
SUVSAVC_00340
SUESAOV_0067
SUJSAA6159_00103(sbnE)
SUKSAA6008_00098(sbnE)
SUCECTR2_76
SUTSAT0131_00106
SUQHMPREF0772_10377
SUZMS7_0112
SUDST398NM01_0132
SUXSAEMRSA15_00860
SUWSATW20_01320(sbnE)
SUGSAPIG0132
SUFSARLGA251_00950(sbnE)
SAUASAAG_00604
SAUERSAU_000074
SAUNSAKOR_00094
SAUSSA40_0087(sbnE)
SAUUSA957_0102(sbnE)
SAUGSA268_0099(sbnE)
SAUZSAZ172_0131(sbnE)
SAUTSAI1T1_2000760
SAUJSAI2T2_1000760
SAUKSAI3T3_1000760
SAUQSAI4T8_1000760
SAUVSAI7S6_1000760
SAUWSAI5S5_1000760
SAUXSAI6T6_1000760
SAUYSAI8T7_1000760
SAUFX998_0099
SABSAB0059
SUYSA2981_0121(sbnE)
SAUBC248_0108
SAUMBN843_1220
SAUCCA347_131
SAURSABB_01720(sbnE)
SAUIAZ30_00625
SAUDCH52_05120
SAMSNI36_00520
SUHSAMSHR1132_00960
SSDSPSINT_0338
SDTSPSE_2120
SDPNCTC12225_02337(iucA)
SHUSHYC_00375(sbnE)
SSCHLH95_00375
SSCZRN70_00595
SAGQEP23_09750
SEQOSE1039_25070
SLZB5P37_07610
SARLSAP2_02070
SSHNCTC13712_00073(iucA_1)
SRAILN051_00250
SFFFOB90_07415
BAGRBA6348_15335
PPOLX809_04485
PTAHPL003_19610
PPEOABE82_04640
PNPIJ22_24510
POWIJ21_46100
PXLBS614_08680
PKBB4V02_14045
PAIHASL14_00120
PPSCEHS13_31660
PBACHUB98_21830
ANXACH33_02505
ATHEK3F53_16445
SACAFFV09_03670
TABCIG75_16795
LFBC1X05_04250
KPULGXN76_14215
PABSJIR001_05130(sbnE)
SACGFDZ84_26450
PMADBAY61_28585
 » show all
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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