KEGG   ENZYME: 6.3.2.58
Entry
EC 6.3.2.58                 Enzyme                                 
Name
D-ornithine---citrate ligase;
sfnaD (gene name)
Class
Ligases;
Forming carbon-nitrogen bonds;
Acid-D-amino-acid ligases (peptide synthases)
Sysname
D-ornithine:citrate ligase {3-[(2-aminopentan-5-oylcarbamoyl)methyl]-3-hydroxybutanoate-forming}
Reaction(IUBMB)
ATP + D-ornithine + citrate = AMP + diphosphate + N5-[(S)-citryl]-D-ornithine [RN:R12353]
Reaction(KEGG)
R12353
Substrate
ATP [CPD:C00002];
D-ornithine [CPD:C00515];
citrate [CPD:C00158]
Product
AMP [CPD:C00020];
diphosphate [CPD:C00013];
N5-[(S)-citryl]-D-ornithine [CPD:C22101]
Comment
Requires Mg2+. The enzyme, characterized from the bacterium Staphylococcus aureus, is involved 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 6.3.2.58 created 2019
Pathway
ec00997  Biosynthesis of various other secondary metabolites
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K23446  D-ornithine---citrate ligase
Genes
SFOZ042_01105
PATREV46_20485
PATOGZ59_41710
PCCPCC21_038990
PPOABJK05_14540
PBRAB5S52_01665
PMRPMI0232
PVLAOB99_03925
PTVAA957_00635
PPSLBJP27_18490
PYMAK972_2775
MVSMVIS_1111
REUReut_B3682
AXNAX27061_3398
AXXERS451415_03381(iucC_2)
SDOSD1155_00635
SBFJCM31447_12920 JCM31447_19990
BWHA9C19_09110
GCTGC56T3_0420
GJFM493_02165
GSRGS3922_13795
HHDHBHAL_4880
HLIHLI_03740
SJEAAV35_000865
MSEMGMB29_11050 GMB29_11055
MCUIG8O30_00930 G8O30_00935
SAUSA1983
SAVSAV2181
SAWSAHV_2165
SAHSaurJH1_2251
SAJSaurJH9_2212
SAMMW2107
SASSAS2082
SARSAR2272
SACSACOL2171
SAXUSA300HOU_2173
SAASAUSA300_2140
SAOSAOUHSC_02436
SAENWMN_2082
SADSAAV_2242
SUUM013TW_2147(sfaD)
SUVSAVC_09775
SUESAOV_2228
SUJSAA6159_02092
SUKSAA6008_02219
SUCECTR2_2042
SUTSAT0131_02350
SUQHMPREF0772_11010
SUZMS7_2204
SUDST398NM01_2241
SUXSAEMRSA15_20860
SUWSATW20_23160
SUGSAPIG2241
SUFSARLGA251_19760
SAUASAAG_00016
SAUERSAU_002025
SAUNSAKOR_02149
SAUSSA40_1936
SAUUSA957_2020
SAUGSA268_2091
SAUZSAZ172_2282
SAUTSAI1T1_2016230
SAUJSAI2T2_1016240
SAUKSAI3T3_1016230
SAUQSAI4T8_1016240
SAUVSAI7S6_1016230
SAUWSAI5S5_1016170
SAUXSAI6T6_1016180
SAUYSAI8T7_1016210
SAUFX998_2166
SABSAB2062
SUYSA2981_2119
SAUBC248_2219
SAUMBN843_22210
SAUCCA347_2266
SAURSABB_01481
SAUIAZ30_11530
SAUDCH52_08040
SAMSNI36_10770
SUHSAMSHR1132_20130
SERSERP1781
SEPSE_1772
SEPPSEB_01781
SEPSDP17_725
SHASH0859
SHHShL2_00752
SSPSSP0705
SCASCA_1684
SSDSPSINT_1843
SDTSPSE_0632
SDPNCTC12225_00705(iucC_1)
SWAA284_03580
SPASSTP1_0610
SXYBE24_08460
SXLSXYLSMQ121_0737
SXOSXYL_00747(sfaD)
SHUSHYC_03395
SCAPAYP1020_1374(iucC)
SSCHLH95_03220
SSCZRN70_03495
SAGQEP23_06680
SEQOSE1039_18710
SSIFAL483_01420
SCVA4G25_11705
SPETCEP67_04920 CEP67_08220
SLZB5P37_02900
SCOHBZ166_07950
SNLBJD96_03850
SKLC7J89_05030
SFQC7J90_00590
SHOMEGX58_07740
SMUSC7J88_05170
SCARDWB96_03745
SCHRDWB92_03195
SARLSAP2_07750
SPICSAMEA4384060_0847(iucC)
SSHNCTC13712_02126(iucC_3)
SSIMSAMEA4384339_2026(iucC_2)
SDBCNQ82_10385
SLLOISP08_03695
SAULI6G39_03095
SSACI6I31_00935
SSCUCEP64_13500
SFFFOB90_04545
MVTI6J10_10600
PANABBH88_04000
PANCE2636_16085
CPASClopa_1242
ASEACPL_4369
AFSAFR_21245
ACTSACWT_4240
PRYPrubr_61750
CATICS0771_66380
SNASnas_3734
HRRHZS55_09375 HZS55_09380
HBOHbor_38340
HTUHtur_0888
HALYHYG82_18640
HSALJMJ58_04535
NAYHYG81_17420
 » 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: 6.3.2.58
IUBMB Enzyme Nomenclature: 6.3.2.58
ExPASy - ENZYME nomenclature database: 6.3.2.58
BRENDA, the Enzyme Database: 6.3.2.58

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