KEGG   ENZYME: 2.1.1.349
Entry
EC 2.1.1.349                Enzyme                                 
Name
toxoflavin synthase;
toxA (gene name)
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
Sysname
S-adenosyl-L-methionine:1,6-didemethyltoxoflavin N1,N6-dimethyltransferase (toxoflavin-forming)
Reaction(IUBMB)
(1) S-adenosyl-L-methionine + 1,6-didemethyltoxoflavin = S-adenosyl-L-homocysteine + reumycin [RN:R12157];
(2) S-adenosyl-L-methionine + reumycin = S-adenosyl-L-homocysteine + toxoflavin [RN:R12158]
Reaction(KEGG)
R12157 R12158
Substrate
S-adenosyl-L-methionine [CPD:C00019];
1,6-didemethyltoxoflavin [CPD:C21956];
reumycin [CPD:C21957]
Product
S-adenosyl-L-homocysteine [CPD:C00021];
reumycin [CPD:C21957];
toxoflavine [CPD:C16789]
Comment
The enzyme is a dual-specificity methyltransferase that catalyses the last two steps of toxoflavin biosynthesis. Toxoflavin is a major virulence factor of several bacterial crop pathogens.
History
EC 2.1.1.349 created 2018
Orthology
K20331  toxoflavin synthase
Genes
SYMK6K13_17790
YAKACZ76_13200 ACZ76_16160
SFJSAMEA4384070_2573
SOFNCTC11214_04378(bioC_2)
PLUplu0250
PLUMA4R40_01225
PAYPAU_03241
PTTVY86_11790
PAKHB0X70_01085
PLUICE143_01085
XBOXBJ1_1516 XBJ1_2779
XBVXBW1_0361 XBW1_0364 XBW1_3521
XNEXNC1_1384 XNC1_2019 XNC1_2445
XNMXNC2_1346 XNC2_1954 XNC2_2352
XDOXDD1_1102(toxA) XDD1_1316 XDD1_1320 XDD1_1508
XPOXPG1_2381 XPG1_2700
XHOA9255_09690 A9255_16450
XBUHGO23_08785 HGO23_13520
PALACO695_02920
BUJBurJV3_3707
STENCCR98_18885
LABLA76x_0657
LAQGLA29479_2850
LCPLC55x_4965
LEZGLE_0529
PMOSO165_012485
PMOLCLJ08_02150
PFLPFL_1036
PPRCPFLCHA0_c10560(toxA)
PPROPPC_1074
PLQAA042_15235
PPVNJ69_03265
PSECCCOS191_2151
PYMAK972_5317
PDWBV82_3620
PXNHU772_015150
PMUYKSS95_17865
PMAMKSS90_10405
PTKEXN22_17150
PTAENCTC10697_01384(toxA)
MCAMCA0484
TTITHITH_10570
HCSFF32_13340
HVNEI420_07645
ADIB5T_03651
BDLAK34_1842 AK34_3761
BGLbglu_2g06400
BGUKS03_5278
BGDbgla_1g04570
BGOBM43_1844
MSDMYSTI_02000 MYSTI_05830
MFBMFUL124B02_06660 MFUL124B02_28840
CCXCOCOR_03369(ubiG4) COCOR_05983
SURSTAUR_6832
AGEAA314_07139
AVMJQX13_49480
MBDMEBOL_006373 MEBOL_006914
CFUSCYFUS_003503 CYFUS_005489 CYFUS_008555
SCUSCE1572_20315
CCROCMC5_053700(ubiE) CMC5_062770(smtA) CMC5_062800(smtA)
MRMA7982_08219 A7982_13440
BICLMTR13_24470
MSCBN69_1794
MBRYB1812_13435
MROSEHO51_00310
AZZDEW08_24275
MULMUL_2739
MMIMMAR_3525 MMAR_3636 MMAR_4425
MMAEMMARE11_34420 MMARE11_35440 MMARE11_42500
MLIMULP_03780
MPSEMPSD_36050 MPSD_45780
MSHOMSHO_02170 MSHO_49470
MSPGF6B93_11885 F6B93_14415
NBRO3I_015605
NTPCRH09_33970
RHWBFN03_03385
SCTSCAT_5482 SCAT_p1624
SCYSCATT_54800 SCATT_p01000
SVESVEN_3943
SDVBN159_1463
SALSSLNWT_7298
SALUDC74_8060
SALLSAZ_41625
SVTSVTN_29985
STREGZL_00343
SLDT261_1553
SLCSL103_16730
STRMM444_06095 M444_32570 M444_36500
SRWTUE45_01220(ubiG_1)
SGSAVL59_28695
SGVB1H19_33505
SALFSMD44_00437
SALJSMD11_0158 SMD11_6408 SMD11_6799
SLXSLAV_32705
STROSTRMOE7_02825
SFKKY5_0115
SKACP970_42325
SGZC0216_16250 C0216_18680
SVNCP980_29715 CP980_30410
SRKFGW37_30550 FGW37_30570 FGW37_30610
SFICEIZ62_09530 EIZ62_31840
SVRCP971_30390
SAQUEJC51_40760
SBYH7H31_01780 H7H31_22130
SRIMCP984_06170 CP984_29705
SSUBCP968_01295 CP968_29700 CP968_29830
SCINCP977_28300
SCHACP983_20860
SGXH4W23_13750
SSPBCP982_02060 CP982_05925 CP982_28355
SNFJYK04_01385(bchM)
SHUNDWB77_07165(ubiG_5)
SCYGS1361_01915
SFEUIM697_31080
SPEUCGZ69_35255
SROIIAG44_03755
SXNIAG42_30705
SACTDMT42_14735
KSKKSE_73110
KAUB6264_23650
SENSACE_7128
AMYCCU254_04900
APRECNX65_23095
AMIAmir_4628
SESPBN6_45550
SSYIEKG83_21765
KPHYAOZ06_29455 AOZ06_31565
LEDBBK82_13205
PLABC6361_36195
PLATC6W10_33740
SYNESyn6312_3678
CYCPCC7424_0911
CYNCyan7425_0895 Cyan7425_3410
OXYHCG48_13190
ANBANA_C12771
GMRGmarT_49760(novO)
GIMF1728_20575
GPNPan110_07630(couO) Pan110_49510(bioC_2)
SDYNMal52_05470(novO)
SRHOHH216_19135
RSIRunsl_2309
RUPDTQ70_28135
FIBA6C57_23755
HTSHMJ29_00435
 » show all
Reference
1  [PMID:27070241]
  Authors
Fenwick MK, Philmus B, Begley TP, Ealick SE
  Title
Burkholderia glumae ToxA Is a Dual-Specificity Methyltransferase That Catalyzes the Last Two Steps of Toxoflavin Biosynthesis.
  Journal
Biochemistry 55:2748-59 (2016)
DOI:10.1021/acs.biochem.6b00167
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 2.1.1.349
IUBMB Enzyme Nomenclature: 2.1.1.349
ExPASy - ENZYME nomenclature database: 2.1.1.349
BRENDA, the Enzyme Database: 2.1.1.349

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