KEGG   ENZYME: 2.3.2.37
Entry
EC 2.3.2.37                 Enzyme                                 
Name
ergosteryl-3beta-O-L-aspartate synthase;
ErdS
Class
Transferases;
Acyltransferases;
Aminoacyltransferases
Sysname
L-aspartyl-tRNAAsp:ergosterol-3beta-O-L-aspartyltransferase
Reaction(IUBMB)
L-aspartyl-tRNAAsp + ergosterol = tRNAAsp + 1-(ergostan-3beta-yl)-L-aspartate [RN:R13187]
Reaction(KEGG)
R13187
Substrate
L-aspartyl-tRNA(Asp) [CPD:C02984];
ergosterol [CPD:C01694]
Product
tRNA(Asp) [CPD:C01638];
1-(ergostan-3beta-yl)-L-aspartate
Comment
The enzyme, detected in fungal species that belong to the Ascomycota and Basidiomycota phyla and characterized from Aspergillus fumigatus, is bifunctional. The AspRS domain catalyses the transfer of L-aspartate to tRNAAsp (EC 6.1.1.12), while the second domain carries out the transfer of L-aspartate to the 3beta-hydroxyl of ergosterol.
History
EC 2.3.2.37 created 2023
Orthology
K24278  ergosteryl-3beta-O-L-aspartate synthase
Genes
NCRNCU07082
NTENEUTE1DRAFT86925(NEUTE1DRAFT_86925)
SMPSMAC_03897
PANPODANSg3375
PBELQC761_405110(DPS1)
PPSDQC762_405110(DPS1)
PPSPQC763_405110(DPS1)
PPSAQC764_405110(DPS1)
TTTTHITE_2109401
MTMMYCTH_59106
MGRMGG_13783
PPEIPpBr36_05421
PGRIPgNI_02914
TMNUCRPA7_4375
FGRFGSG_01976
FPUFPSE_09210
FPOAFPOAC1_002103
FVNFVRRES_02346
FVRFVEG_07262
FOXFOXG_04148 FOXG_16675 FOXG_16738
NHENECHADRAFT_96752
FFCNCS54_01271900
FKRNCS57_01237500
FMUJ7337_010725
TRETRIREDRAFT_48819
TRRM419DRAFT_110431
MAWMAC_06778
MAJMAA_01125
PCHMVFPPC_03564
CMTCCM_02981
AMUSLMH87_006953
PLJVFPFJ_00684
PTKZJDV02_007963(DPS1)
VALVDBG_03134
VDAVDAG_02041
CFJCFIO01_08749
CLUPCLUP02_06618
CHIGCH63R_01433
ELAUCREL1_7942
PFYPFICI_05047
SSLSS1G_11475
BFUBCIN_08g05800
MBEMBM_03824
PSCOLY89DRAFT_656573
GLZGLAREA_06461
ANIANIA_00314
AFMAFUA_1G02570
ACTACLA_031840
NFINFIA_022050
AORAO090005000838
ANGAn01g05630
AFVAFLA_003657
ALUCAKAW2_20668S
ACHEACHE_11809S
APUUAPUU_11796A
PCSN7525_004213
PDPPDIP_63500
POUPOX_b03344
TMFEYB26_008489
TRGTRUGW13939_00066
CIMCIMG_04731
CPWCPC735_071000
UREUREG_06784
PBLPAAG_05664
PBNPADG_07732
ABEARB_01269
TVETRV_01140
AJEHCAG_04705
BGHBDBG_04515
PNOSNOG_04267
PTEPTT_11927
BZECOCCADRAFT_7647
BSCCOCSADRAFT_37947
BORCOCMIDRAFT_80535
AALTCC77DRAFT_833387
ARABEKO05_0002150
ZTRMYCGRDRAFT_53676
PFJMYCFIDRAFT_160086
FFUCLAFUR5_00532
CBETCB0940_01174
BCOMBAUCODRAFT_37211
NPAUCRNP2_4367
CNECNG00400
CNBCNBG4380
CNGCNAG_03563
CGICGB_G6320C
CDEUCNBG_2059
TVSTRAVEDRAFT_62662
DSQDICSQDRAFT_137523
PCOPHACADRAFT_118899
SHSSTEHIDRAFT_135399
PSQPUNSTDRAFT_125466
ADLAURDEDRAFT_143959
GTRGLOTRDRAFT_131655
MRRMoror_5228
MOREE1B28_003413
SCMSCHCO_01196424(SCHCODRAFT_01196424)
UMAUMAG_10270
PFPPFL1_06798
SGRAEX895_003994
MGLMGL_0589
MRTMRET_4297
MSYMMSY001_2768
 » show all
Reference
1  [PMID:32541034]
  Authors
Yakobov N, Fischer F, Mahmoudi N, Saga Y, Grube CD, Roy H, Senger B, Grob G, Tatematsu S, Yokokawa D, Mouyna I, Latge JP, Nakajima H, Kushiro T, Becker HD
  Title
RNA-dependent sterol aspartylation in fungi.
  Journal
Proc Natl Acad Sci U S A 117:14948-14957 (2020)
DOI:10.1073/pnas.2003266117
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 2.3.2.37
IUBMB Enzyme Nomenclature: 2.3.2.37
ExPASy - ENZYME nomenclature database: 2.3.2.37
BRENDA, the Enzyme Database: 2.3.2.37

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