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DLKcat/DeeplearningApproach/Data/EC_enzyme/enzclass.txt ADDED
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1
+ ---------------------------------------------------------------------------
2
+ ENZYME nomenclature database
3
+ SIB Swiss Institute of Bioinformatics; Geneva, Switzerland
4
+ ---------------------------------------------------------------------------
5
+
6
+ Description: ENZYME class hierarchy
7
+ Name: enzclass.txt
8
+ Release: 17-Jun-2020
9
+
10
+ ---------------------------------------------------------------------------
11
+
12
+ 1. -. -.- Oxidoreductases.
13
+ 1. 1. -.- Acting on the CH-OH group of donors.
14
+ 1. 1. 1.- With NAD(+) or NADP(+) as acceptor.
15
+ 1. 1. 2.- With a cytochrome as acceptor.
16
+ 1. 1. 3.- With oxygen as acceptor.
17
+ 1. 1. 4.- With a disulfide as acceptor.
18
+ 1. 1. 5.- With a quinone or similar compound as acceptor.
19
+ 1. 1. 9.- With a copper protein as acceptor.
20
+ 1. 1.98.- With other, known, acceptors.
21
+ 1. 1.99.- With other acceptors.
22
+ 1. 2. -.- Acting on the aldehyde or oxo group of donors.
23
+ 1. 2. 1.- With NAD(+) or NADP(+) as acceptor.
24
+ 1. 2. 2.- With a cytochrome as acceptor.
25
+ 1. 2. 3.- With oxygen as acceptor.
26
+ 1. 2. 4.- With a disulfide as acceptor.
27
+ 1. 2. 5.- With a quinone or similar compound as acceptor.
28
+ 1. 2. 7.- With an iron-sulfur protein as acceptor.
29
+ 1. 2.98.- With other, known, acceptors.
30
+ 1. 2.99.- With other acceptors.
31
+ 1. 3. -.- Acting on the CH-CH group of donors.
32
+ 1. 3. 1.- With NAD(+) or NADP(+) as acceptor.
33
+ 1. 3. 2.- With a cytochrome as acceptor.
34
+ 1. 3. 3.- With oxygen as acceptor.
35
+ 1. 3. 4.- With a disulfide as acceptor.
36
+ 1. 3. 5.- With a quinone or related compound as acceptor.
37
+ 1. 3. 7.- With an iron-sulfur protein as acceptor.
38
+ 1. 3. 8.- With a flavin as acceptor.
39
+ 1. 3.98.- With other, known, acceptors.
40
+ 1. 3.99.- With other acceptors.
41
+ 1. 4. -.- Acting on the CH-NH(2) group of donors.
42
+ 1. 4. 1.- With NAD(+) or NADP(+) as acceptor.
43
+ 1. 4. 2.- With a cytochrome as acceptor.
44
+ 1. 4. 3.- With oxygen as acceptor.
45
+ 1. 4. 4.- With a disulfide as acceptor.
46
+ 1. 4. 5.- With a quinone or similar compound as acceptor.
47
+ 1. 4. 7.- With an iron-sulfur protein as acceptor.
48
+ 1. 4. 9.- With a copper protein as acceptor.
49
+ 1. 4.98.- With other, known, acceptors.
50
+ 1. 4.99.- With other acceptors.
51
+ 1. 5. -.- Acting on the CH-NH group of donors.
52
+ 1. 5. 1.- With NAD(+) or NADP(+) as acceptor.
53
+ 1. 5. 3.- With oxygen as acceptor.
54
+ 1. 5. 4.- With a disulfide as acceptor.
55
+ 1. 5. 5.- With a quinone or similar compound as acceptor.
56
+ 1. 5. 7.- With an iron-sulfur protein as acceptor.
57
+ 1. 5. 8.- With a flavin as acceptor.
58
+ 1. 5.98.- With other, known, acceptors.
59
+ 1. 5.99.- With other acceptors.
60
+ 1. 6. -.- Acting on NADH or NADPH.
61
+ 1. 6. 1.- With NAD(+) or NADP(+) as acceptor.
62
+ 1. 6. 2.- With a heme protein as acceptor.
63
+ 1. 6. 3.- With oxygen as acceptor.
64
+ 1. 6. 4.- With a disulfide as acceptor.
65
+ 1. 6. 5.- With a quinone or similar compound as acceptor.
66
+ 1. 6. 6.- With a nitrogenous group as acceptor.
67
+ 1. 6. 7.- With a iron-sulfur protein as acceptor.
68
+ 1. 6. 8.- With a flavin as acceptor.
69
+ 1. 6.99.- With other acceptors.
70
+ 1. 7. -.- Acting on other nitrogenous compounds as donors.
71
+ 1. 7. 1.- With NAD(+) or NADP(+) as acceptor.
72
+ 1. 7. 2.- With a cytochrome as acceptor.
73
+ 1. 7. 3.- With oxygen as acceptor.
74
+ 1. 7. 5.- With a quinone or similar compound as acceptor.
75
+ 1. 7. 6.- With a nitrogenous group as acceptor.
76
+ 1. 7. 7.- With an iron-sulfur protein as acceptor.
77
+ 1. 7. 9.- With a copper protein as acceptor.
78
+ 1. 7.99.- With other acceptors.
79
+ 1. 8. -.- Acting on a sulfur group of donors.
80
+ 1. 8. 1.- With NAD(+) or NADP(+) as acceptor.
81
+ 1. 8. 2.- With a cytochrome as acceptor.
82
+ 1. 8. 3.- With oxygen as acceptor.
83
+ 1. 8. 4.- With a disulfide as acceptor.
84
+ 1. 8. 5.- With a quinone or similar compound as acceptor.
85
+ 1. 8. 6.- With an nitrogenous group as acceptor.
86
+ 1. 8. 7.- With an iron-sulfur protein as acceptor.
87
+ 1. 8.98.- With other, known, acceptors.
88
+ 1. 8.99.- With other acceptors.
89
+ 1. 9. -.- Acting on a heme group of donors.
90
+ 1. 9. 3.- With oxygen as acceptor.
91
+ 1. 9. 6.- With a nitrogenous group as acceptor.
92
+ 1. 9.98.- With other, known, acceptors.
93
+ 1. 9.99.- With other acceptors.
94
+ 1.10. -.- Acting on diphenols and related substances as donors.
95
+ 1.10. 1.- With NAD(+) or NADP(+) as acceptor.
96
+ 1.10. 2.- With a cytochrome as acceptor.
97
+ 1.10. 3.- With oxygen as acceptor.
98
+ 1.10. 5.- With a quinone or related compound as acceptor.
99
+ 1.10. 9.- With a copper protein as acceptor.
100
+ 1.10.98.- With other, known, acceptors.
101
+ 1.10.99.- With other acceptors.
102
+ 1.11. -.- Acting on a peroxide as acceptor.
103
+ 1.11. 1.- Peroxidases.
104
+ 1.11. 2.- With H(2)O(2) as acceptor, one oxygen atom of which is incorporated into the product.
105
+ 1.12. -.- Acting on hydrogen as donors.
106
+ 1.12. 1.- With NAD(+) or NADP(+) as acceptor.
107
+ 1.12. 2.- With a cytochrome as acceptor.
108
+ 1.12. 5.- With a quinone or similar compound as acceptor.
109
+ 1.12. 7.- With an iron-sulfur protein as acceptor.
110
+ 1.12.98.- With other, known, acceptors.
111
+ 1.12.99.- With other acceptors.
112
+ 1.13. -.- Acting on single donors with incorporation of molecular oxygen (oxygenases). The oxygen incorporated need not be derived from O(2).
113
+ 1.13. 1.- With NADH or NADPH as one donor.
114
+ 1.13.11.- With incorporation of two atoms of oxygen.
115
+ 1.13.12.- With incorporation of one atom of oxygen (internal monooxygenases or internal mixed function oxidases).
116
+ 1.13.99.- Miscellaneous.
117
+ 1.14. -.- Acting on paired donors, with incorporation or reduction of molecular oxygen. The oxygen incorporated need not be derived from O(2).
118
+ 1.14. 1.- With NADH or NADPH as one donor.
119
+ 1.14. 2.- With ascorbate as one donor.
120
+ 1.14. 3.- With reduced pteridine as one donor.
121
+ 1.14.11.- With 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors.
122
+ 1.14.12.- With NADH or NADPH as one donor, and incorporation of two atoms of oxygen into one donor.
123
+ 1.14.13.- With NADH or NADPH as one donor, and incorporation of one atom of oxygen.
124
+ 1.14.14.- With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen.
125
+ 1.14.15.- With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen.
126
+ 1.14.16.- With reduced pteridine as one donor, and incorporation of one atom of oxygen.
127
+ 1.14.17.- With reduced ascorbate as one donor, and incorporation of one atom of oxygen.
128
+ 1.14.18.- With another compound as one donor, and incorporation of one atom of oxygen.
129
+ 1.14.19.- With oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water.
130
+ 1.14.20.- With 2-oxoglutarate as one donor, and the other dehydrogenated.
131
+ 1.14.21.- With NADH or NADPH as one donor, and the other dehydrogenated.
132
+ 1.14.99.- Miscellaneous.
133
+ 1.15. -.- Acting on superoxide as acceptor.
134
+ 1.15. 1.- Acting on superoxide as acceptor.
135
+ 1.16. -.- Oxidizing metal ions.
136
+ 1.16. 1.- With NAD(+) or NADP(+) as acceptor.
137
+ 1.16. 3.- With oxygen as acceptor.
138
+ 1.16. 5.- With a quinone or similar compound as acceptor.
139
+ 1.16. 8.- With a flavin as acceptor.
140
+ 1.16. 9.- With a copper protein as acceptor.
141
+ 1.16.98.- With other known acceptors.
142
+ 1.17. -.- Acting on CH or CH(2) groups.
143
+ 1.17. 1.- With NAD(+) or NADP(+) as acceptor.
144
+ 1.17. 2.- With a cytochrome as acceptor.
145
+ 1.17. 3.- With oxygen as acceptor.
146
+ 1.17. 4.- With a disulfide as acceptor.
147
+ 1.17. 5.- With a quinone or similar compound as acceptor.
148
+ 1.17. 7.- With an iron-sulfur protein as acceptor.
149
+ 1.17. 8.- With a flavin as acceptor.
150
+ 1.17. 9.- With a copper protein as acceptor.
151
+ 1.17.98.- With other, known, acceptors.
152
+ 1.17.99.- With other acceptors.
153
+ 1.18. -.- Acting on iron-sulfur proteins as donors.
154
+ 1.18. 1.- With NAD(+) or NADP(+) as acceptor.
155
+ 1.18. 2.- With dinitrogen as acceptor.
156
+ 1.18. 3.- With H(+) as acceptor.
157
+ 1.18. 6.- With dinitrogen as acceptor.
158
+ 1.18.96.- With other, known, acceptors.
159
+ 1.18.99.- With H(+) as acceptor.
160
+ 1.19. -.- Acting on reduced flavodoxin as donor.
161
+ 1.19. 1.- With NAD(+) or NADP(+) as acceptor.
162
+ 1.19. 6.- With dinitrogen as acceptor.
163
+ 1.20. -.- Acting on phosphorus or arsenic in donors.
164
+ 1.20. 1.- With NAD(+) or NADP(+) as acceptor.
165
+ 1.20. 2.- With a cytochrome as acceptor.
166
+ 1.20. 4.- With disulfide as acceptor.
167
+ 1.20. 9.- With a copper protein as acceptor.
168
+ 1.20.98.- With other, known acceptors.
169
+ 1.20.99.- With other acceptors.
170
+ 1.21. -.- Catalyzing the reaction X-H + Y-H = 'X-Y'.
171
+ 1.21. 1.- With NAD(+) or NADP(+) as acceptor.
172
+ 1.21. 3.- With oxygen as acceptor.
173
+ 1.21. 4.- With a disulfide as acceptor.
174
+ 1.21.98.- With other, known acceptors.
175
+ 1.21.99.- With other acceptors.
176
+ 1.22. -.- Acting on halogen in donors.
177
+ 1.22. 1.- With NAD(+) or NADP(+) as acceptor.
178
+ 1.23. -.- Reducing C-O-C group as acceptor.
179
+ 1.23. 1.- With NADH or NADPH as donor.
180
+ 1.23. 5.- With a quinone or similar compound as acceptor.
181
+ 1.97. -.- Other oxidoreductases.
182
+ 1.97. 1.- Other oxidoreductases.
183
+ 1.98. -.- Enzymes using H(2) as reductant.
184
+ 1.98. 1.- Other oxidoreductases.
185
+ 1.99. -.- Other enzymes using O(2) as oxidant.
186
+ 1.99. 1.- Hydroxylases.
187
+ 1.99. 2.- Oxygenases.
188
+
189
+ 2. -. -.- Transferases.
190
+ 2. 1. -.- Transferring one-carbon groups.
191
+ 2. 1. 1.- Methyltransferases.
192
+ 2. 1. 2.- Hydroxymethyl-, formyl- and related transferases.
193
+ 2. 1. 3.- Carboxy- and carbamoyltransferases.
194
+ 2. 1. 4.- Amidinotransferases.
195
+ 2. 1. 5.- Methylenetransferases.
196
+ 2. 2. -.- Transferring aldehyde or ketonic groups.
197
+ 2. 2. 1.- Transketolases and transaldolases.
198
+ 2. 3. -.- Acyltransferases.
199
+ 2. 3. 1.- Transferring groups other than amino-acyl groups.
200
+ 2. 3. 2.- Aminoacyltransferases.
201
+ 2. 3. 3.- Acyl groups converted into alkyl groups on transfer.
202
+ 2. 4. -.- Glycosyltransferases.
203
+ 2. 4. 1.- Hexosyltransferases.
204
+ 2. 4. 2.- Pentosyltransferases.
205
+ 2. 4.99.- Transferring other glycosyl groups.
206
+ 2. 5. -.- Transferring alkyl or aryl groups, other than methyl groups.
207
+ 2. 5. 1.- Transferring alkyl or aryl groups, other than methyl groups.
208
+ 2. 6. -.- Transferring nitrogenous groups.
209
+ 2. 6. 1.- Transaminases.
210
+ 2. 6. 2.- Amidinotransferases.
211
+ 2. 6. 3.- Oximinotransferases.
212
+ 2. 6.99.- Transferring other nitrogenous groups.
213
+ 2. 7. -.- Transferring phosphorus-containing groups.
214
+ 2. 7. 1.- Phosphotransferases with an alcohol group as acceptor.
215
+ 2. 7. 2.- Phosphotransferases with a carboxy group as acceptor.
216
+ 2. 7. 3.- Phosphotransferases with a nitrogenous group as acceptor.
217
+ 2. 7. 4.- Phosphotransferases with a phosphate group as acceptor.
218
+ 2. 7. 5.- Phosphotransferases with regeneration of donors, apparently catalyzing intramolecular transfers.
219
+ 2. 7. 6.- Diphosphotransferases.
220
+ 2. 7. 7.- Nucleotidyltransferases.
221
+ 2. 7. 8.- Transferases for other substituted phosphate groups.
222
+ 2. 7. 9.- Phosphotransferases with paired acceptors.
223
+ 2. 7.10.- Protein-tyrosine kinases.
224
+ 2. 7.11.- Protein-serine/threonine kinases.
225
+ 2. 7.12.- Dual-specificity kinases (those acting on Ser/Thr and Tyr residues).
226
+ 2. 7.13.- Protein-histidine kinases.
227
+ 2. 7.14.- Protein-arginine kinases.
228
+ 2. 7.99.- Other protein kinases.
229
+ 2. 8. -.- Transferring sulfur-containing groups.
230
+ 2. 8. 1.- Sulfurtransferases.
231
+ 2. 8. 2.- Sulfotransferases.
232
+ 2. 8. 3.- CoA-transferases.
233
+ 2. 8. 4.- Transferring alkylthio groups.
234
+ 2. 8. 5.- Thiosulfotransferases.
235
+ 2. 9. -.- Transferring selenium-containing groups.
236
+ 2. 9. 1.- Selenotransferases.
237
+ 2.10. -.- Transferring molybdenum- or tungsten-containing groups.
238
+ 2.10. 1.- Molybdenumtransferases or tungstentransferases with sulfide groups as acceptors.
239
+
240
+ 3. -. -.- Hydrolases.
241
+ 3. 1. -.- Acting on ester bonds.
242
+ 3. 1. 1.- Carboxylic ester hydrolases.
243
+ 3. 1. 2.- Thiolester hydrolases.
244
+ 3. 1. 3.- Phosphoric monoester hydrolases.
245
+ 3. 1. 4.- Phosphoric diester hydrolases.
246
+ 3. 1. 5.- Triphosphoric monoester hydrolases.
247
+ 3. 1. 6.- Sulfuric ester hydrolases.
248
+ 3. 1. 7.- Diphosphoric monoester hydrolases.
249
+ 3. 1. 8.- Phosphoric triester hydrolases.
250
+ 3. 1.11.- Exodeoxyribonucleases producing 5'-phosphomonoesters.
251
+ 3. 1.12.- Exodeoxyribonucleases producing 3'-phosphomonoesters.
252
+ 3. 1.13.- Exoribonucleases producing 5'-phosphomonoesters.
253
+ 3. 1.14.- Exoribonucleases producing 3'-phosphomonoesters.
254
+ 3. 1.15.- Exonucleases active with either ribo- or deoxyribonucleic acids and producing 5'-phosphomonoesters.
255
+ 3. 1.16.- Exonucleases active with either ribo- or deoxyribonucleic acids and producing 3'-phosphomonoesters.
256
+ 3. 1.21.- Endodeoxyribonucleases producing 5'-phosphomonoesters.
257
+ 3. 1.22.- Endodeoxyribonucleases producing other than 5'-phosphomonoesters.
258
+ 3. 1.23.- Site specific endodeoxyribonucleases: cleavage is sequence specific.
259
+ 3. 1.24.- Site specific endodeoxyribonucleases: cleavage is not sequence specific.
260
+ 3. 1.25.- Site-specific endodeoxyribonucleases specific for altered bases.
261
+ 3. 1.26.- Endoribonucleases producing 5'-phosphomonoesters.
262
+ 3. 1.27.- Endoribonucleases producing other than 5'-phosphomonoesters.
263
+ 3. 1.30.- Endoribonucleases active with either ribo- or deoxyribonucleic acids and producing 5'-phosphomonoesters.
264
+ 3. 1.31.- Endoribonucleases active with either ribo- or deoxyribonucleic acids and producing 3'-phosphomonoesters.
265
+ 3. 2. -.- Glycosylases.
266
+ 3. 2. 1.- Glycosidases, i.e. enzymes hydrolyzing O- and S-glycosyl compounds.
267
+ 3. 2. 2.- Hydrolyzing N-glycosyl compounds.
268
+ 3. 2. 3.- Hydrolyzing S-glycosyl compounds.
269
+ 3. 3. -.- Acting on ether bonds.
270
+ 3. 3. 1.- Thioether and trialkylsulfonium hydrolases.
271
+ 3. 3. 2.- Ether hydrolases.
272
+ 3. 4. -.- Acting on peptide bonds (peptidases).
273
+ 3. 4. 1.- alpha-Amino-acyl-peptide hydrolases.
274
+ 3. 4. 2.- Peptidyl-amino-acid hydrolases.
275
+ 3. 4. 3.- Dipeptide hydrolases.
276
+ 3. 4. 4.- Peptidyl peptide hydrolases.
277
+ 3. 4.11.- Aminopeptidases.
278
+ 3. 4.12.- Peptidylamino-acid hydrolases or acylamino-acid hydrolases.
279
+ 3. 4.13.- Dipeptidases.
280
+ 3. 4.14.- Dipeptidyl-peptidases and tripeptidyl-peptidases.
281
+ 3. 4.15.- Peptidyl-dipeptidases.
282
+ 3. 4.16.- Serine-type carboxypeptidases.
283
+ 3. 4.17.- Metallocarboxypeptidases.
284
+ 3. 4.18.- Cysteine-type carboxypeptidases.
285
+ 3. 4.19.- Omega peptidases.
286
+ 3. 4.21.- Serine endopeptidases.
287
+ 3. 4.22.- Cysteine endopeptidases.
288
+ 3. 4.23.- Aspartic endopeptidases.
289
+ 3. 4.24.- Metalloendopeptidases.
290
+ 3. 4.25.- Threonine endopeptidases.
291
+ 3. 4.99.- Endopeptidases of unknown catalytic mechanism.
292
+ 3. 5. -.- Acting on carbon-nitrogen bonds, other than peptide bonds.
293
+ 3. 5. 1.- In linear amides.
294
+ 3. 5. 2.- In cyclic amides.
295
+ 3. 5. 3.- In linear amidines.
296
+ 3. 5. 4.- In cyclic amidines.
297
+ 3. 5. 5.- In nitriles.
298
+ 3. 5.99.- In other compounds.
299
+ 3. 6. -.- Acting on acid anhydrides.
300
+ 3. 6. 1.- In phosphorus-containing anhydrides.
301
+ 3. 6. 2.- In sulfonyl-containing anhydrides.
302
+ 3. 6. 3.- Acting on acid anhydrides; catalyzing transmembrane movement of substances.
303
+ 3. 6. 4.- Acting on ATP; involved in cellular and subcellular movement.
304
+ 3. 6. 5.- Acting on GTP; involved in cellular and subcellular movement.
305
+ 3. 7. -.- Acting on carbon-carbon bonds.
306
+ 3. 7. 1.- In ketonic substances.
307
+ 3. 8. -.- Acting on halide bonds.
308
+ 3. 8. 1.- In C-halide compounds.
309
+ 3. 8. 2.- In P-halide compounds.
310
+ 3. 9. -.- Acting on phosphorus-nitrogen bonds.
311
+ 3. 9. 1.- Acting on phosphorus-nitrogen bonds.
312
+ 3.10. -.- Acting on sulfur-nitrogen bonds.
313
+ 3.10. 1.- Acting on sulfur-nitrogen bonds.
314
+ 3.11. -.- Acting on carbon-phosphorus bonds.
315
+ 3.11. 1.- Acting on carbon-phosphorus bonds.
316
+ 3.12. -.- Acting on sulfur-sulfur bonds.
317
+ 3.12. 1.- Acting on sulfur-sulfur bonds.
318
+ 3.13. -.- Acting on carbon-sulfur bonds.
319
+ 3.13. 1.- Acting on carbon-sulfur bonds.
320
+
321
+ 4. -. -.- Lyases.
322
+ 4. 1. -.- Carbon-carbon lyases.
323
+ 4. 1. 1.- Carboxy-lyases.
324
+ 4. 1. 2.- Aldehyde-lyases.
325
+ 4. 1. 3.- Oxo-acid-lyases.
326
+ 4. 1.99.- Other carbon-carbon lyases.
327
+ 4. 2. -.- Carbon-oxygen lyases.
328
+ 4. 2. 1.- Hydro-lyases.
329
+ 4. 2. 2.- Acting on polysaccharides.
330
+ 4. 2. 3.- Acting on phosphates.
331
+ 4. 2.99.- Other carbon-oxygen lyases.
332
+ 4. 3. -.- Carbon-nitrogen lyases.
333
+ 4. 3. 1.- Ammonia-lyases.
334
+ 4. 3. 2.- Lyases acting on amides, amidines, etc.
335
+ 4. 3. 3.- Amine-lyases.
336
+ 4. 3.99.- Other carbon-nitrogen lyases.
337
+ 4. 4. -.- Carbon-sulfur lyases.
338
+ 4. 4. 1.- Carbon-sulfur lyases.
339
+ 4. 5. -.- Carbon-halide lyases.
340
+ 4. 5. 1.- Carbon-halide lyases.
341
+ 4. 6. -.- Phosphorus-oxygen lyases.
342
+ 4. 6. 1.- Phosphorus-oxygen lyases.
343
+ 4. 7. -.- Carbon-phosphorus lyases.
344
+ 4. 7. 1.- Carbon-phosphorus lyases.
345
+ 4.99. -.- Other lyases.
346
+ 4.99. 1.- Other lyases.
347
+
348
+ 5. -. -.- Isomerases.
349
+ 5. 1. -.- Racemases and epimerases.
350
+ 5. 1. 1.- Acting on amino acids and derivatives.
351
+ 5. 1. 2.- Acting on hydroxy acids and derivatives.
352
+ 5. 1. 3.- Acting on carbohydrates and derivatives.
353
+ 5. 1.99.- Acting on other compounds.
354
+ 5. 2. -.- Cis-trans-isomerases.
355
+ 5. 2. 1.- Cis-trans isomerases.
356
+ 5. 3. -.- Intramolecular oxidoreductases.
357
+ 5. 3. 1.- Interconverting aldoses and ketoses.
358
+ 5. 3. 2.- Interconverting keto- and enol-groups.
359
+ 5. 3. 3.- Transposing C=C bonds.
360
+ 5. 3. 4.- Transposing S-S bonds.
361
+ 5. 3.99.- Other intramolecular oxidoreductases.
362
+ 5. 4. -.- Intramolecular transferases.
363
+ 5. 4. 1.- Transferring acyl groups.
364
+ 5. 4. 2.- Phosphotransferases (phosphomutases).
365
+ 5. 4. 3.- Transferring amino groups.
366
+ 5. 4. 4.- Transferring hydroxy groups.
367
+ 5. 4.99.- Transferring other groups.
368
+ 5. 5. -.- Intramolecular lyases.
369
+ 5. 5. 1.- Intramolecular lyases.
370
+ 5. 6. -.- Isomerases altering macromolecular conformation.
371
+ 5. 6. 1.- Enzymes altering polypeptide conformation or assembly.
372
+ 5. 6. 2.- Enzymes altering nucleic acid conformation.
373
+ 5.99. -.- Other isomerases.
374
+ 5.99. 1.- Other isomerases.
375
+
376
+ 6. -. -.- Ligases.
377
+ 6. 1. -.- Forming carbon-oxygen bonds.
378
+ 6. 1. 1.- Ligases forming aminoacyl-tRNA and related compounds.
379
+ 6. 1. 2.- Acid--alcohol ligases (ester synthases).
380
+ 6. 1. 3.- Cyclo-ligases.
381
+ 6. 2. -.- Forming carbon-sulfur bonds.
382
+ 6. 2. 1.- Acid--thiol ligases.
383
+ 6. 3. -.- Forming carbon-nitrogen bonds.
384
+ 6. 3. 1.- Acid--ammonia (or amine) ligases (amide synthases).
385
+ 6. 3. 2.- Acid--amino-acid ligases (peptide synthases).
386
+ 6. 3. 3.- Cyclo-ligases.
387
+ 6. 3. 4.- Other carbon--nitrogen ligases.
388
+ 6. 3. 5.- Carbon--nitrogen ligases with glutamine as amido-N-donor.
389
+ 6. 4. -.- Forming carbon-carbon bonds.
390
+ 6. 4. 1.- Forming carbon-carbon bonds.
391
+ 6. 5. -.- Forming phosphoric ester bonds.
392
+ 6. 5. 1.- Forming phosphoric ester bonds.
393
+ 6. 6. -.- Forming nitrogen-metal bonds.
394
+ 6. 6. 1.- Forming coordination complexes.
395
+
396
+ 7. -. -.- Translocases.
397
+ 7. 1. -.- Catalysing the translocation of hydrons.
398
+ 7. 1. 1.- Hydron translocation or charge separation linked to oxidoreductase reactions.
399
+ 7. 1. 2.- Hydron translocation linked to the hydrolysis of a nucleoside triphosphate.
400
+ 7. 1. 3.- Hydron translocation linked to the hydrolysis of diphosphate.
401
+ 7. 2. -.- Catalysing the translocation of inorganic cations.
402
+ 7. 2. 1.- Linked to oxidoreductase reactions.
403
+ 7. 2. 2.- Linked to the hydrolysis of a nucleoside triphosphate.
404
+ 7. 2. 3.- Linked to the hydrolysis of diphosphate.
405
+ 7. 2. 4.- Linked to decarboxylation.
406
+ 7. 3. -.- Catalysing the translocation of inorganic anions and their chelates.
407
+ 7. 3. 2.- Linked to the hydrolysis of a nucleoside triphosphate.
408
+ 7. 4. -.- Catalysing the translocation amino acids and peptides.
409
+ 7. 4. 2.- Linked to the hydrolysis of a nucleoside triphosphate.
410
+ 7. 5. -.- Catalysing the translocation carbohydrates and their derivatives.
411
+ 7. 5. 2.- Linked to the hydrolysis of a nucleoside triphosphate.
412
+ 7. 6. -.- Catalysing the translocation of other compounds.
413
+ 7. 6. 2.- Linked to the hydrolysis of a nucleoside triphosphate.
414
+
415
+ ---------------------------------------------------------------------------
416
+ Copyrighted by the SIB Swiss Institute of Bioinformatics and
417
+ distributed under the Creative Commons Attribution (CC BY 4.0) License
418
+ ---------------------------------------------------------------------------