KEGG   ENZYME: 6.2.2.3
Entry
EC 6.2.2.3                  Enzyme                                 
Name
thiazoline synthase
Class
Ligases;
Forming carbon-sulfur bonds;
Amide---thiol ligases
Sysname
[protein]-(L-amino acyl-L-cysteine) cyclodehydratase (2-thiazoline-forming)
Reaction(IUBMB)
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-cysteine)
Product
ADP [CPD:C00008];
phosphate [CPD:C00009];
[protein]-(1S,4R)-2-(C-substituted-aminomethyl)-4-acyl-2-thiazoline
Comment
Requires Mg2+. The enzyme, which participates in the biosynthesis of some ribosomal peptide natural products (RiPPs) such as the trunkamides, converts L-cysteine residues to thiazoline rings. 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 L-cysteine 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. This activity is also catalysed by the related enzyme EC 6.2.2.2, oxazoline synthase. That enzyme differs by having an RRE domain that also recognizes L-serine and L-threonine residues, which are converted to oxazoline and methyloxazoline rings, respectively.
History
EC 6.2.2.3 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:20540059]
  Authors
McIntosh JA, Schmidt EW
  Title
Marine molecular machines: heterocyclization in cyanobactin biosynthesis.
  Journal
Chembiochem 11:1413-21 (2010)
DOI:10.1002/cbic.201000196
Reference
2  [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
3  [PMID:24214017]
  Authors
Koehnke J, Bent AF, Zollman D, Smith K, Houssen WE, Zhu X, Mann G, Lebl T, Scharff R, Shirran S, Botting CH, Jaspars M, Schwarz-Linek U, Naismith JH
  Title
The cyanobactin heterocyclase enzyme: a processive adenylase that operates with a defined order of reaction.
  Journal
Angew Chem Int Ed Engl 52:13991-6 (2013)
DOI:10.1002/anie.201306302
Reference
4  [PMID:26098679]
  Authors
Koehnke J, Mann G, Bent AF, Ludewig H, Shirran S, Botting C, Lebl T, Houssen W, Jaspars M, Naismith JH
  Title
Structural analysis of leader peptide binding enables leader-free cyanobactin processing.
  Journal
Nat Chem Biol 11:558-563 (2015)
DOI:10.1038/nchembio.1841
Reference
5  [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
Other DBs
ExplorEnz - The Enzyme Database: 6.2.2.3
IUBMB Enzyme Nomenclature: 6.2.2.3
ExPASy - ENZYME nomenclature database: 6.2.2.3
BRENDA, the Enzyme Database: 6.2.2.3

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