29:
1531:
398:
244:
578:
ATP:cob(I)alamin adenosyltransferases are classed into three groups: CobA-type, EutT-type and PduO-type. Each of the three enzyme types appears to be specialised for particular AdoCbl-dependent
1119:
985:
Suh SJ, Escalante-Semerena JC (July 1993). "Cloning, sequencing and overexpression of cobA which encodes ATP:corrinoid adenosyltransferase in
Salmonella typhimurium".
497:
356:
198:
217:
1112:
1192:
1022:"Glycerol conversion to 1,3-propanediol by Clostridium pasteurianum: cloning and expression of the gene encoding 1,3-propanediol dehydrogenase"
445:
304:
1105:
938:"Functional genomic, biochemical, and genetic characterization of the Salmonella pduO gene, an ATP:cob(I)alamin adenosyltransferase gene"
630:
ring, necessary for the conversion of cobalamin to adenosylcobalamin. PduO functions to convert cobalamin to AdoCbl for 1,2-propanediol
1250:
1202:
1063:"Purification and initial biochemical characterization of ATP:Cob(I)alamin adenosyltransferase (EutT) enzyme of Salmonella enterica"
1212:
210:
1167:
161:
137:
1406:
517:
376:
1157:
889:"The eutT gene of Salmonella enterica Encodes an oxygen-labile, metal-containing ATP:corrinoid adenosyltransferase enzyme"
1521:
1391:
1579:
1507:
1494:
1481:
1468:
1455:
1442:
1429:
1217:
1187:
1149:
1401:
155:
1355:
1298:
1177:
1140:
534:
48:
505:
364:
248:
the three-dimensional structure of atp:corrinoid adenosyltransferase from salmonella typhimurium. apo-atp form
142:
1303:
557:
788:"Evidence that a B12-adenosyl transferase is encoded within the ethanolamine operon of Salmonella enterica"
666:
631:
603:
840:"Studies of the CobA-type ATP:Co(I)rrinoid adenosyltransferase enzyme of Methanosarcina mazei strain Go1"
222:
1324:
1243:
130:
1396:
501:
360:
65:
595:
458:
317:
1360:
1207:
1182:
1172:
158:
60:
736:"Multiple roles of ATP:cob(I)alamin adenosyltransferases in the conversion of B12 to coenzyme B12"
82:
1293:
619:
587:
1584:
1197:
1084:
1043:
1002:
967:
918:
869:
817:
765:
716:
583:
553:
492:
351:
149:
1339:
1334:
1308:
1236:
1074:
1033:
994:
957:
949:
908:
900:
859:
851:
807:
799:
755:
747:
706:
698:
484:
343:
118:
1386:
1370:
1283:
626:. CobA is responsible for attaching the adenosyl moiety from ATP to the cobalt ion of the
533:(also known as ATP:cob(I)alamin adenosyltransferase or ATP:corrinoid adenosyltransferase)
94:
1097:
53:
1535:
1424:
1365:
864:
839:
760:
735:
711:
686:
193:
1038:
1021:
913:
888:
812:
787:
173:
28:
1573:
1329:
1288:
998:
962:
937:
904:
855:
803:
450:
309:
168:
953:
426:
272:
1278:
635:
591:
480:
339:
285:
1565:
1551:
438:
297:
1502:
1437:
1273:
1128:
609:
177:
1530:
936:
Johnson CL, Pechonick E, Park SD, Havemann GD, Leal NA, Bobik TA (March 2001).
1162:
751:
1476:
1450:
549:
1088:
1079:
1062:
971:
922:
873:
821:
769:
720:
1047:
1006:
454:
397:
313:
243:
1561:
1547:
572:
545:
433:
402:
crystal structure of conserved protein 0546 from thermoplasma acidophilum
292:
601:
The CobA group includes the ATP:cob(I)alamin adenosyltransferases CobA (
537:
106:
623:
579:
125:
33:
Human mitochondrial Cob(I)yrinic acid a,c-diamide adenosyltransferase,
702:
1489:
1259:
1132:
627:
565:
561:
541:
512:
371:
205:
101:
89:
77:
786:
Sheppard DE, Penrod JT, Bobik T, Kofoid E, Roth JR (November 2004).
1463:
1557:
1543:
1136:
687:"Structure of ATP-bound human ATP:cobalamin adenosyltransferase"
474:
421:
333:
279:
267:
113:
34:
1232:
1101:
1020:
Luers F, Seyfried M, Daniel R, Gottschalk G (September 1997).
586:
of AdoCbl. PduO and EutT are distantly related, sharing short
568:
556:(coenzyme B12, AdoCbl). Adenosylcobalamin is required as a
1228:
887:
Buan NR, Suh SJ, Escalante-Semerena JC (September 2004).
1556:
This article incorporates text from the public domain
1542:
This article incorporates text from the public domain
838:
Buan NR, Rehfeld K, Escalante-Semerena JC (May 2006).
1519:
564:. AdoCbl contains an adenosyl moiety liganded to the
1415:
1379:
1348:
1317:
1266:
1148:
511:
491:
473:
468:
444:
432:
420:
412:
407:
390:
370:
350:
332:
327:
303:
291:
278:
266:
258:
253:
236:
216:
204:
192:
187:
167:
148:
136:
124:
112:
100:
88:
76:
71:
59:
47:
42:
21:
734:Mera PE, Escalante-Semerena JC (September 2010).
531:cob(I)yrinic acid a,c-diamide adenosyltransferase
833:
831:
781:
779:
552:(vitamin B12) into one of its coenzyme forms,
1244:
1113:
8:
1061:Buan NR, Escalante-Semerena JC (June 2006).
1251:
1237:
1229:
1120:
1106:
1098:
465:
396:
324:
242:
184:
27:
1078:
1037:
961:
912:
863:
811:
759:
710:
391:Cobalamin adenosyltransferase (PduO/EutT)
1193:Farnesyl-diphosphate farnesyltransferase
1526:
677:
685:Schubert HL, Hill CP (December 2006).
387:
233:
18:
7:
653:ATP:cob(I)alamin adenosyltransferase
14:
1203:Alkylglycerone phosphate synthase
656:ATP:corrinoid adenosyltransferase
634:, while EutT produces AdoCbl for
237:ATP:corrinoid adenosyltransferase
22:ATP:corrinoid adenosyltransferase
1529:
1213:Geranylgeranyltransferase type 1
905:10.1128/JB.186.17.5708-5714.2004
856:10.1128/JB.188.10.3543-3550.2006
804:10.1128/JB.186.22.7635-7644.2004
954:10.1128/JB.183.5.1577-1584.2001
594:unrelated and is an example of
1168:Methionine adenosyltransferase
646:This enzyme is also known as:
1:
1158:Dimethylallyltranstransferase
1039:10.1016/s0378-1097(97)00351-0
650:Cobalamin adenosyltransferase
618:). There is a high degree of
469:Available protein structures:
328:Available protein structures:
999:10.1016/0378-1119(93)90701-4
560:for the activity of certain
740:Appl. Microbiol. Biotechnol
1601:
1555:
1541:
1407:Michaelis–Menten kinetics
1218:Porphobilinogen deaminase
1188:Glutathione S-transferase
752:10.1007/s00253-010-2773-2
464:
395:
323:
241:
183:
26:
1299:Diffusion-limited enzyme
1178:Dihydropteroate synthase
622:identity between these
1080:10.1074/jbc.M603069200
667:Cobalamin biosynthesis
604:Salmonella typhimurium
590:motifs, while CobA is
529:In molecular biology,
1392:Eadie–Hofstee diagram
1325:Allosteric regulation
1402:Lineweaver–Burk plot
1026:FEMS Microbiol. Lett
596:convergent evolution
1208:Farnesyltransferase
1183:Spermidine synthase
1173:Riboflavin synthase
571:of cobalamin via a
1361:Enzyme superfamily
1294:Enzyme promiscuity
548:the conversion of
1517:
1516:
1226:
1225:
1198:Spermine synthase
703:10.1021/bi061396f
584:de novo synthesis
554:adenosylcobalamin
527:
526:
523:
522:
518:structure summary
386:
385:
382:
381:
377:structure summary
232:
231:
228:
227:
131:metabolic pathway
1592:
1580:Protein families
1534:
1533:
1525:
1397:Hanes–Woolf plot
1340:Enzyme activator
1335:Enzyme inhibitor
1309:Enzyme catalysis
1253:
1246:
1239:
1230:
1122:
1115:
1108:
1099:
1093:
1092:
1082:
1058:
1052:
1051:
1041:
1017:
1011:
1010:
982:
976:
975:
965:
933:
927:
926:
916:
884:
878:
877:
867:
835:
826:
825:
815:
783:
774:
773:
763:
731:
725:
724:
714:
697:(51): 15188–96.
682:
616:Escherichia coli
466:
400:
388:
325:
246:
234:
185:
31:
19:
16:Class of enzymes
1600:
1599:
1595:
1594:
1593:
1591:
1590:
1589:
1570:
1569:
1568:
1554:
1540:
1528:
1520:
1518:
1513:
1425:Oxidoreductases
1411:
1387:Enzyme kinetics
1375:
1371:List of enzymes
1344:
1313:
1284:Catalytic triad
1262:
1257:
1227:
1222:
1144:
1126:
1096:
1073:(25): 16971–7.
1060:
1059:
1055:
1019:
1018:
1014:
984:
983:
979:
935:
934:
930:
899:(17): 5708–14.
886:
885:
881:
850:(10): 3543–50.
837:
836:
829:
798:(22): 7635–44.
785:
784:
777:
733:
732:
728:
684:
683:
679:
675:
663:
644:
416:Cob_adeno_trans
403:
249:
38:
17:
12:
11:
5:
1598:
1596:
1588:
1587:
1582:
1572:
1571:
1539:
1538:
1515:
1514:
1512:
1511:
1498:
1485:
1472:
1459:
1446:
1433:
1419:
1417:
1413:
1412:
1410:
1409:
1404:
1399:
1394:
1389:
1383:
1381:
1377:
1376:
1374:
1373:
1368:
1363:
1358:
1352:
1350:
1349:Classification
1346:
1345:
1343:
1342:
1337:
1332:
1327:
1321:
1319:
1315:
1314:
1312:
1311:
1306:
1301:
1296:
1291:
1286:
1281:
1276:
1270:
1268:
1264:
1263:
1258:
1256:
1255:
1248:
1241:
1233:
1224:
1223:
1221:
1220:
1215:
1210:
1205:
1200:
1195:
1190:
1185:
1180:
1175:
1170:
1165:
1160:
1154:
1152:
1146:
1145:
1127:
1125:
1124:
1117:
1110:
1102:
1095:
1094:
1053:
1012:
977:
948:(5): 1577–84.
928:
879:
827:
775:
726:
676:
674:
671:
670:
669:
662:
659:
658:
657:
654:
651:
643:
640:
592:evolutionarily
525:
524:
521:
520:
515:
509:
508:
495:
489:
488:
478:
471:
470:
462:
461:
448:
442:
441:
436:
430:
429:
424:
418:
417:
414:
410:
409:
405:
404:
401:
393:
392:
384:
383:
380:
379:
374:
368:
367:
354:
348:
347:
337:
330:
329:
321:
320:
307:
301:
300:
295:
289:
288:
283:
276:
275:
270:
264:
263:
262:CobA_CobO_BtuR
260:
256:
255:
251:
250:
247:
239:
238:
230:
229:
226:
225:
220:
214:
213:
208:
202:
201:
196:
190:
189:
181:
180:
171:
165:
164:
153:
146:
145:
140:
134:
133:
128:
122:
121:
116:
110:
109:
104:
98:
97:
92:
86:
85:
80:
74:
73:
69:
68:
63:
57:
56:
51:
45:
44:
40:
39:
32:
24:
23:
15:
13:
10:
9:
6:
4:
3:
2:
1597:
1586:
1583:
1581:
1578:
1577:
1575:
1567:
1563:
1559:
1553:
1549:
1545:
1537:
1532:
1527:
1523:
1509:
1505:
1504:
1499:
1496:
1492:
1491:
1486:
1483:
1479:
1478:
1473:
1470:
1466:
1465:
1460:
1457:
1453:
1452:
1447:
1444:
1440:
1439:
1434:
1431:
1427:
1426:
1421:
1420:
1418:
1414:
1408:
1405:
1403:
1400:
1398:
1395:
1393:
1390:
1388:
1385:
1384:
1382:
1378:
1372:
1369:
1367:
1366:Enzyme family
1364:
1362:
1359:
1357:
1354:
1353:
1351:
1347:
1341:
1338:
1336:
1333:
1331:
1330:Cooperativity
1328:
1326:
1323:
1322:
1320:
1316:
1310:
1307:
1305:
1302:
1300:
1297:
1295:
1292:
1290:
1289:Oxyanion hole
1287:
1285:
1282:
1280:
1277:
1275:
1272:
1271:
1269:
1265:
1261:
1254:
1249:
1247:
1242:
1240:
1235:
1234:
1231:
1219:
1216:
1214:
1211:
1209:
1206:
1204:
1201:
1199:
1196:
1194:
1191:
1189:
1186:
1184:
1181:
1179:
1176:
1174:
1171:
1169:
1166:
1164:
1161:
1159:
1156:
1155:
1153:
1151:
1147:
1142:
1138:
1134:
1130:
1123:
1118:
1116:
1111:
1109:
1104:
1103:
1100:
1090:
1086:
1081:
1076:
1072:
1068:
1067:J. Biol. Chem
1064:
1057:
1054:
1049:
1045:
1040:
1035:
1032:(2): 337–45.
1031:
1027:
1023:
1016:
1013:
1008:
1004:
1000:
996:
992:
988:
981:
978:
973:
969:
964:
959:
955:
951:
947:
943:
939:
932:
929:
924:
920:
915:
910:
906:
902:
898:
894:
890:
883:
880:
875:
871:
866:
861:
857:
853:
849:
845:
841:
834:
832:
828:
823:
819:
814:
809:
805:
801:
797:
793:
789:
782:
780:
776:
771:
767:
762:
757:
753:
749:
745:
741:
737:
730:
727:
722:
718:
713:
708:
704:
700:
696:
692:
688:
681:
678:
672:
668:
665:
664:
660:
655:
652:
649:
648:
647:
641:
639:
638:utilisation.
637:
633:
629:
625:
621:
617:
614:), and ButR (
613:
612:denitrificans
611:
606:
605:
599:
597:
593:
589:
585:
581:
576:
574:
570:
567:
563:
559:
555:
551:
547:
543:
539:
536:
532:
519:
516:
514:
510:
507:
503:
499:
496:
494:
490:
486:
482:
479:
476:
472:
467:
463:
460:
456:
452:
449:
447:
443:
440:
437:
435:
431:
428:
425:
423:
419:
415:
411:
406:
399:
394:
389:
378:
375:
373:
369:
366:
362:
358:
355:
353:
349:
345:
341:
338:
335:
331:
326:
322:
319:
315:
311:
308:
306:
302:
299:
296:
294:
290:
287:
284:
281:
277:
274:
271:
269:
265:
261:
257:
252:
245:
240:
235:
224:
221:
219:
215:
212:
209:
207:
203:
200:
197:
195:
191:
186:
182:
179:
175:
172:
170:
169:Gene Ontology
166:
163:
160:
157:
154:
151:
147:
144:
141:
139:
135:
132:
129:
127:
123:
120:
117:
115:
111:
108:
107:NiceZyme view
105:
103:
99:
96:
93:
91:
87:
84:
81:
79:
75:
70:
67:
64:
62:
58:
55:
52:
50:
46:
41:
36:
30:
25:
20:
1503:Translocases
1500:
1487:
1474:
1461:
1448:
1438:Transferases
1435:
1422:
1279:Binding site
1163:Thiaminase I
1129:Transferases
1070:
1066:
1056:
1029:
1025:
1015:
990:
986:
980:
945:
942:J. Bacteriol
941:
931:
896:
893:J. Bacteriol
892:
882:
847:
844:J. Bacteriol
843:
795:
792:J. Bacteriol
791:
743:
739:
729:
694:
691:Biochemistry
690:
680:
645:
636:ethanolamine
615:
608:
602:
600:
577:
530:
528:
95:BRENDA entry
1274:Active site
993:(1): 93–7.
746:(1): 41–8.
632:degradation
610:Pseudomonas
582:or for the
575:Co-C bond.
408:Identifiers
254:Identifiers
83:IntEnz view
66:37277-84-2
43:Identifiers
1574:Categories
1477:Isomerases
1451:Hydrolases
1318:Regulation
673:References
481:structures
340:structures
152:structures
119:KEGG entry
1566:IPR002779
1552:IPR003724
1356:EC number
607:), CobO (
588:conserved
550:cobalamin
546:catalyses
439:IPR002779
298:IPR003724
72:Databases
1585:EC 2.5.1
1562:InterPro
1548:InterPro
1380:Kinetics
1304:Cofactor
1267:Activity
1089:16636051
972:11160088
923:15317775
874:16672609
822:15516577
770:20677021
721:17176040
661:See also
642:Synonyms
624:proteins
620:sequence
573:covalent
558:cofactor
538:2.5.1.17
498:RCSB PDB
434:InterPro
357:RCSB PDB
293:InterPro
223:proteins
211:articles
199:articles
156:RCSB PDB
54:2.5.1.17
1536:Biology
1490:Ligases
1260:Enzymes
1048:9311132
1007:7916712
865:1482872
761:3034633
712:2532598
580:enzymes
562:enzymes
427:PF01923
273:PF02572
178:QuickGO
143:profile
126:MetaCyc
61:CAS no.
1522:Portal
1464:Lyases
1087:
1046:
1005:
970:
960:
921:
914:516830
911:
872:
862:
820:
813:524904
810:
768:
758:
719:
709:
628:corrin
566:cobalt
544:which
542:enzyme
540:is an
513:PDBsum
487:
477:
459:SUPFAM
413:Symbol
372:PDBsum
346:
336:
318:SUPFAM
286:CL0023
259:Symbol
206:PubMed
188:Search
174:AmiGO
162:PDBsum
102:ExPASy
90:BRENDA
78:IntEnz
49:EC no.
1416:Types
1150:2.5.1
1133:alkyl
963:95042
455:SCOPe
446:SCOP2
314:SCOPe
305:SCOP2
138:PRIAM
1560:and
1558:Pfam
1546:and
1544:Pfam
1508:list
1501:EC7
1495:list
1488:EC6
1482:list
1475:EC5
1469:list
1462:EC4
1456:list
1449:EC3
1443:list
1436:EC2
1430:list
1423:EC1
1143:2.5)
1137:aryl
1135:and
1085:PMID
1044:PMID
1003:PMID
987:Gene
968:PMID
919:PMID
870:PMID
818:PMID
766:PMID
717:PMID
506:PDBj
502:PDBe
485:ECOD
475:Pfam
451:1nog
422:Pfam
365:PDBj
361:PDBe
344:ECOD
334:Pfam
310:1g64
282:clan
280:Pfam
268:Pfam
218:NCBI
159:PDBe
114:KEGG
35:MMAB
1075:doi
1071:281
1034:doi
1030:154
995:doi
991:129
958:PMC
950:doi
946:183
909:PMC
901:doi
897:186
860:PMC
852:doi
848:188
808:PMC
800:doi
796:186
756:PMC
748:doi
707:PMC
699:doi
569:ion
493:PDB
352:PDB
194:PMC
150:PDB
1576::
1564::
1550::
1141:EC
1131::
1083:.
1069:.
1065:.
1042:.
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1024:.
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966:.
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764:.
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742:.
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535:EC
504:;
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1252:e
1245:t
1238:v
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1107:v
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