KEGG   ENZYME: 6.2.2.2
Entry
EC 6.2.2.2                  Enzyme                                 
Name
oxazoline synthase;
cyanobactin heterocyclase;
cyanobactin cyclodehydratase;
patD (gene name);
balhD (gene name);
micD (gene name)
Class
Ligases;
Forming carbon-sulfur bonds;
Amide---thiol ligases
Sysname
[protein]-(L-amino acyl-L-serine) cyclodehydratase (2-oxazoline-forming)
Reaction(IUBMB)
(1) ATP + a [protein]-(L-amino acyl-L-serine) = ADP + phosphate + a [protein]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-2-oxazoline;
(2) ATP + a [protein]-(L-amino acyl-L-threonine) = ADP + phosphate + a [protein]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-5-methyl-2-oxazoline;
(3) ATP + a [protein]-(L-amino acyl-L-cysteine) = ADP + phosphate + a [protein]-(1S,4R)-2-(C-substituted-aminomethyl)-4-acyl-2-thiazoline
Substrate
ATP [CPD:C00002];
[protein]-(L-amino acyl-L-serine);
[protein]-(L-amino acyl-L-threonine);
[protein]-(L-amino acyl-L-cysteine)
Product
ADP [CPD:C00008];
phosphate [CPD:C00009];
[protein]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-2-oxazoline;
[protein]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-5-methyl-2-oxazoline;
[protein]-(1S,4R)-2-(C-substituted-aminomethyl)-4-acyl-2-thiazoline
Comment
Requires Mg2+. The enzyme, which participates in the biosynthesis of ribosomal peptide natural products (RiPPs), converts L-cysteine, L-serine and L-threonine residues to thiazoline, oxazoline, and methyloxazoline rings, respectively. The enzyme requires two domains - a cyclodehydratase domain, known as a YcaO domain, and a substrate recognition domain (RRE domain) that controls the regiospecificity of the enzyme. The RRE domain can either be fused to the YcaO domain or occur as a separate protein; however both domains are required for activity. The enzyme can process multiple residues within the same substrate peptide, and all enzymes characterized so far follow a defined order, starting with the L-cysteine closest to the C-terminus. The reaction involves phosphorylation of the preceding ribosomal peptide backbone amide bond, forming ADP and a phosphorylated intermediate, followed by release of the phosphate group. In some cases the enzyme catalyses a side reaction in which the phosphorylated intermediate reacts with ADP to form AMP and diphosphate.
History
EC 6.2.2.2 created 2020
Orthology
K24411  oxazoline/thiazoline synthase
Genes
PGBH744_2c1844
PRRAT705_20070
PVBJ5X90_21760
MARQMARGE09_P0853
MPSYCEK71_11635
TIGTHII_1452
AQLBXU06_00280
BMABMA0023
BMVBMASAVP1_A2869
BMLBMA10229_A2214
BMNBMA10247_2493
BMALDM55_418
BMAEDM78_499
BMAQDM76_398
BMAIDM57_2183
BMAFDM51_3009
BMAZBM44_807
BMABBM45_414
BPSBPSL0600
BPMBURPS1710b_0802
BPLBURPS1106A_0637
BPDBURPS668_0622
BPRGBP346_A0549
BPSEBDL_1405
BPSMBBQ_2827
BPSDBBX_3353
BPZBP1026B_I2930
BPQBPC006_I0625
BPKBBK_886
BPSHDR55_494
BPSABBU_1551
BPSOX996_101
BUTX994_2115
BTEBTH_I0517
BTQBTQ_539
BTJBTJ_1946
BTZBTL_3182
BTDBTI_3187
BTVBTHA_3465
BTHEBTN_1530
BTHMBTRA_60
BTHADR62_1717
BTHLBG87_25
BOKDM82_26
BOCBG90_995
BUUWS70_14740
BSAVWS86_15990
BHGI6G56_04185
BCMBcenmc03_4504
BCHBcen2424_5723
BCJBCAM0032
BCEOI35_4032
BAMBamb_4992
BACBamMC406_3135
BCEDDM42_5115
BPYRABD05_21225
BSEMWJ12_25405
BSTGWT74_32040
BARINLX30_22710
BULBW21_3336
BUDAQ610_15965
BURKDM992_26160
PTSCUJ90_29050
PMEGFNZ07_00045
AAVAave_3061
AAAAcav_2221
DACDaci_4368
DELDelCs14_2459
DHKBO996_19610
DLAI6G47_02440
VAMC4F17_30355
DEKDSLASN_28920
CCXCOCOR_04620
SURSTAUR_1663
AGEAA314_02212
CFUSCYFUS_000837
SCLsce0227 sce5176
SCUSCE1572_02015 SCE1572_30100
CCROCMC5_033250 CMC5_081770(cyaA)
MRMA7982_03398 A7982_06091
SATSYN_00274
BJAblr4538(blr4538)
BJUBJ6T_51450
BJPRN69_25080
BRKCWS35_23610
BGZXH91_06895
BARHWN72_25870 WN72_46055
BSEPHAP48_0039290
BQBJ4P68_0038540
BBANJ4G43_027305
STARG3545_22485
METM446_3967
MNOMnod_4676
MLGCWB41_13610
MSCBN69_1551
MBRYB1812_20390
MROSEHO51_01070
SHUMSTHU_40390
NAOY958_24450 Y958_24465
THACCSC3H3_22235
TABCIG75_17290
JEPBW721_03320
SWOSwol_1788
DORDesor_3762
CANSGP473_07770
NNONONO_c00050
SALBXNR_3461
SCBSCAB_63151
SSXSACTE_1726
SVLStrvi_8159
SRCM271_30830
SMALSMALA_2873
SBHSBI_06840
SVESVEN_6223
SCIB446_13300
SVTSVTN_18875
SRWTUE45_01307
STRFASR50_01150 ASR50_34290
SCLFBB341_25495
SGSAVL59_01395
SALWCP975_34200
SAUOBV401_18015
SPUNBFF78_19325
SLAUSLA_3079
SLKSLUN_04620 SLUN_33425
SCYAEJ357_00390 EJ357_47540
SGZC0216_07565 C0216_15285
SVNCP980_11010
SNKCP967_10280
SRKFGW37_00455
SFICEIZ62_03870
SGALCP966_28965
SVRCP971_15250
SSUBCP968_16040 CP968_16620
SGXH4W23_11665
SHUNDWB77_05178
SFEUIM697_37575
SDWK7C20_32740
SXNIAG42_22290
SANUK7396_04330
SACTDMT42_14025
SRUGF0345_11985
KSKKSE_27520 KSE_45670
KABB7C62_31245
KAUB6264_10285
KITCFP65_2554 CFP65_4131
KISHUT16_21095 HUT16_23660
MLVCVS47_02157(ycaO)
RIAC7V51_03980
LMOIVV02_06540
ARUBJ5A65_02050
THAONI17_021795
STRREKD16_18460
TCUTcur_2767
NGNLCN96_33510
AMDAMED_5949 AMED_6889
AMNRAM_30510 RAM_35345
AMMAMES_5866 AMES_6783
AMZB737_5866 B737_6783
AOIAORI_1830
AJAAJAP_30310
AMYCCU254_40720
AMYBBKN51_01365
AABA4R43_37025
AMYYYIM_41055
AORISD37_32060
APRTMUY14_02100 MUY14_06110
AROONQK81_13800
SSYIEKG83_30540
KPHYAOZ06_20905
ALOCRK57519
ACTUActkin_03742
MSAGGCM10017556_24710
VMAVAB18032_20050
CATICS0771_44570
DVCDvina_40855
DMATDmats_35695
NAVJQS30_10125 JQS30_10130
AEYCDG81_20685
SYNKKR100_09760
WNAKA717_21735
KOVK9N68_13665
MARMAE_33130
MPKVL20_3234
MVZmyaer102_08530
CYTcce_4099
CYCPCC7424_5737
CYJCyan7822_0614 Cyan7822_6146 Cyan7822_6152 Cyan7822_6535
CYNCyan7425_0519
TERTery_2355
ARPNIES39_O01120
MICMic7113_1028
OACOscil6304_5209
ONIOsc7112_3651
MPROBJP34_23205 BJP34_35410
NFLCOO91_08369 COO91_10280
NOECLI64_06955 CLI64_08520
ACYAnacy_0374
CSGCylst_1148
RSINB6N60_05272
CALTCal6303_5683
CALNNIES2098_57630
RIVRiv7116_6334
TOQHCG51_32110
NCNBZZ01_09385
PLPPle7327_1615
LCREPla8534_19280
FTJFTUN_1196
TPHGFUT81_08155
PFERIRI77_02400
SCORJ3U87_25370
FNFBSQ88_05055
AQAD1815_13425
AQDD1816_11250
CCAUEG346_15190
PLTPlut_0880
 » show all
Reference
1  [PMID:20210311]
  Authors
McIntosh JA, Donia MS, Schmidt EW
  Title
Insights into heterocyclization from two highly similar enzymes.
  Journal
J Am Chem Soc 132:4089-91 (2010)
DOI:10.1021/ja9107116
Reference
2  [PMID:22401305]
  Authors
Melby JO, Dunbar KL, Trinh NQ, Mitchell DA
  Title
Selectivity, directionality, and promiscuity in peptide processing from a Bacillus sp. Al Hakam cyclodehydratase.
  Journal
J Am Chem Soc 134:5309-16 (2012)
DOI:10.1021/ja211675n
Reference
3  [PMID:30912640]
  Authors
Ge Y, Czekster CM, Miller OK, Botting CH, Schwarz-Linek U, Naismith JH
  Title
Insights into the Mechanism of the Cyanobactin Heterocyclase Enzyme.
  Journal
Biochemistry 58:2125-2132 (2019)
DOI:10.1021/acs.biochem.9b00084
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 6.2.2.2
IUBMB Enzyme Nomenclature: 6.2.2.2
ExPASy - ENZYME nomenclature database: 6.2.2.2
BRENDA, the Enzyme Database: 6.2.2.2

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