KEGG   ENZYME: 6.3.2.57
Entry
EC 6.3.2.57                 Enzyme                                 
Name
staphyloferrin A synthase;
sfnaB (gene name)
Class
Ligases;
Forming carbon-nitrogen bonds;
Acid-D-amino-acid ligases (peptide synthases)
Sysname
N5-[(S)-citryl]-D-ornithine:citrate ligase (staphyloferrin A-forming)
Reaction(IUBMB)
ATP + N5-[(S)-citryl]-D-ornithine + citrate = AMP + diphosphate + staphyloferrin A [RN:R12354]
Reaction(KEGG)
R12354
Substrate
ATP [CPD:C00002];
N5-[(S)-citryl]-D-ornithine [CPD:C22101];
citrate [CPD:C00158]
Product
AMP [CPD:C00020];
diphosphate [CPD:C00013];
staphyloferrin A [CPD:C22102]
Comment
Requires Mg2+. The enzyme, characterized from the bacterium Staphylococcus aureus, catalyses the last step in the biosynthesis of the siderophore staphyloferrin A. 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 6.3.2.57 created 2019
Pathway
ec00997  Biosynthesis of various other secondary metabolites
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K23447  staphyloferrin A synthase
Genes
LPNlpg1325(frgA)
LPHLPV_1432(FrgA)
LPOLPO_1303(FrgA)
LPULPE509_01881
LPMLP6_1307(frgA)
LPFlpl1279
LPPlpp1280
LPCLPC_0740(frgA)
LPAlpa_01955
LPElp12_1263
LLOLLO_3129(FrgA)
LHALHA_3006(FrgA)
LCDclem_01380(iucC)
LSHCAB17_02135
LLG44548918_02520(iucC)
LGTE4T54_08065
SDOSD1155_00625
BWHA9C19_09105
BARDQRY57_10050
GCTGC56T3_0421
GJFM493_02170
GSRGS3922_13790
HHDHBHAL_4881(figA)
HLIHLI_03745
SJEAAV35_000860
SAUSA1981
SAVSAV2179
SAWSAHV_2163
SAHSaurJH1_2249
SAJSaurJH9_2210
SAMMW2105
SASSAS2080
SARSAR2270
SACSACOL2169
SAXUSA300HOU_2171
SAASAUSA300_2138
SAOSAOUHSC_02434
SAENWMN_2080
SADSAAV_2240
SUUM013TW_2145(sfaB)
SUVSAVC_09765
SUESAOV_2226c
SUJSAA6159_02090(sfaB)
SUKSAA6008_02217
SUCECTR2_2040
SUTSAT0131_02348
SUQHMPREF0772_11012
SUZMS7_2202
SUDST398NM01_2239
SUXSAEMRSA15_20840
SUWSATW20_23140
SUGSAPIG2239
SUFSARLGA251_19740
SAUASAAG_00014
SAUERSAU_002023
SAUNSAKOR_02147
SAUSSA40_1934
SAUUSA957_2018
SAUGSA268_2089
SAUZSAZ172_2280
SAUTSAI1T1_2016210
SAUJSAI2T2_1016220
SAUKSAI3T3_1016210
SAUQSAI4T8_1016220
SAUVSAI7S6_1016210
SAUWSAI5S5_1016150
SAUXSAI6T6_1016160
SAUYSAI8T7_1016190
SAUFX998_2164
SABSAB2060c
SUYSA2981_2117
SAUBC248_2217
SAUMBN843_22190
SAUCCA347_2264
SAURSABB_01483
SAUIAZ30_11520
SAUDCH52_08050
SAMSNI36_10760
SUHSAMSHR1132_20110
SERSERP1779
SEPSE_1770
SEPPSEB_01779
SEPSDP17_723
SHASH0861
SHHShL2_00754
SSPSSP0707
SCASCA_1682
SLGSLGD_00838
SLNSLUG_08960
SSDSPSINT_1841
SDTSPSE_0634
SDPNCTC12225_00707(iucC_2)
SWAA284_03590
SPASSTP1_0608
SXYBE24_08450
SXLSXYLSMQ121_0739
SXOSXYL_00749(sfaB)
SHUSHYC_03405
SCAPAYP1020_1372(iucA)
SSCHLH95_03230
SSCZRN70_03505
SAGQEP23_06670
SEQOSE1039_18700
SSIFAL483_01430
SCVA4G25_11715
SPETCEP67_04915 CEP67_08225
SLZB5P37_02890
SCOHBZ166_07960
SNLBJD96_03860
SKLC7J89_05040
SFQC7J90_00580
SHOMEGX58_07745
SMUSC7J88_05160
SCARDWB96_03755
SCHRDWB92_03205
SARLSAP2_07760
SPICSAMEA4384060_0849(iucA)
SSHNCTC13712_02124(iucA_2)
SSIMSAMEA4384339_2024(iucC_1)
SDBCNQ82_10375
SLLOISP08_03705
SAULI6G39_03105
SSACI6I31_00925
SRAILN051_02925
SPSDJMB28_04195
STASHYI43_04045
SURYMUA21_09200
SEDAMNY58_03760
SCAQQMO72_03705
SDEVQ2T90_03615
SROTML435_10450
STAPAOB58_2564
SSCUCEP64_13505
SFFFOB90_04535
SSTESAMEA4384403_0110(iucC) SAMEA4384403_0111(iucA)
MVTI6J10_10595
PANABBH88_03995
PANCE2636_16090
ASEACPL_4368
AMSAMIS_41860
ACTNL083_3994
ACTSACWT_4239
PFLAPflav_024190
PSUUPsuf_079590
PRYPrubr_61740
CATICS0771_66370
SNASnas_3733
NAVJQS30_07795 JQS30_07800
GLYK3N28_09090
FPCFPSM_02589
FPYFPG101_12935
FPQIB65_12400
FPVIA03_12175
FPWIA04_12060
FPKIA06_12135
 » show all
Reference
1  [PMID:19138128]
  Authors
Cotton JL, Tao J, Balibar CJ
  Title
Identification and characterization of the Staphylococcus aureus gene cluster coding for staphyloferrin A.
  Journal
Biochemistry 48:1025-35 (2009)
DOI:10.1021/bi801844c
Other DBs
ExplorEnz - The Enzyme Database: 6.3.2.57
IUBMB Enzyme Nomenclature: 6.3.2.57
ExPASy - ENZYME nomenclature database: 6.3.2.57
BRENDA, the Enzyme Database: 6.3.2.57

DBGET integrated database retrieval system