KEGG   ENZYME: 2.5.1.154
Entry
EC 2.5.1.154                Enzyme                                 
Name
corrinoid adenosyltransferase EutT;
eutT (gene name)
Class
Transferases;
Transferring alkyl or aryl groups, other than methyl groups;
Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
Sysname
ATP:cob(II)alamin Cobeta-adenosyltransferase (diphosphate-forming)
Reaction(IUBMB)
2 ATP + 2 cob(II)alamin + a reduced flavoprotein = 2 diphosphate + 2 phosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein (overall reaction) [RN:R12945];
(1a) 2 cob(II)alamin + 2 [corrinoid adenosyltransferase] = 2 [corrinoid adenosyltransferase]-cob(II)alamin;
(1b) a reduced flavoprotein + 2 [corrinoid adenosyltransferase]-cob(II)alamin = an oxidized flavoprotein + 2 [corrinoid adenosyltransferase]-cob(I)alamin (spontaneous);
(1c) 2 ATP + 2 [corrinoid adenosyltransferase]-cob(I)alamin = 2 diphosphate + 2 phosphate + 2 adenosylcob(III)alamin + 2 [corrinoid adenosyltransferase]
Reaction(KEGG)
R12945;
(other) R01492
Substrate
ATP [CPD:C00002];
cob(II)alamin [CPD:C00541];
reduced flavoprotein [CPD:C03024];
[corrinoid adenosyltransferase];
[corrinoid adenosyltransferase]-cob(II)alamin;
[corrinoid adenosyltransferase]-cob(I)alamin
Product
diphosphate [CPD:C00013];
phosphate [CPD:C00009];
adenosylcob(III)alamin [CPD:C00194];
oxidized flavoprotein [CPD:C03161];
[corrinoid adenosyltransferase]-cob(II)alamin;
[corrinoid adenosyltransferase]-cob(I)alamin (spontaneous);
[corrinoid adenosyltransferase]
Comment
The corrinoid adenosylation pathway comprises three steps: (i) reduction of Co(III) within the corrinoid to Co(II) by a one-electron transfer. This can occur non-enzymically in the presence of dihydroflavin nucleotides or reduced flavoproteins [1]. (ii) Co(II) is bound by corrinoid adenosyltransferase, resulting in displacement of the lower axial ligand by an aromatic residue. The reduction potential of the 4-coordinate Co(II) intermediate is raised by ~250 mV compared with the free compound, bringing it to within physiological range. This is followed by a second single-electron transfer from either free dihydroflavins or the reduced flavin cofactor of flavoproteins, resulting in reduction to Co(I) [4]. (iii) the Co(I) conducts a nucleophilic attack on the adenosyl moiety of ATP, resulting in transfer of the deoxyadenosyl group and oxidation of the cobalt atom to Co(III) state. Three types of corrinoid adenosyltransferases, not related by sequence, have been described. In the anaerobic bacterium Salmonella enterica they are encoded by the cobA gene (a housekeeping enzyme involved in both the de novo biosynthesis and the salvage of adenosylcobalamin), the pduO gene (involved in (S)-propane-1,2-diol utilization), and the eutT gene (involved in ethanolamine utilization). The first two types, which produce triphosphate, are classified as EC 2.5.1.17, corrinoid adenosyltransferase, while the EutT type hydrolyses triphosphate to diphosphate and phosphate during catalysis and is thus classified separately.
History
EC 2.5.1.154 created 2021
Pathway
ec00860  Porphyrin metabolism
ec01100  Metabolic pathways
Orthology
K04032  ethanolamine utilization cobalamin adenosyltransferase
Genes
ECOb2459(eutT)
ECJJW2443(eutT)
ECDECDH10B_2624(eutT)
EBWBWG_2221(eutT)
ECOKECMDS42_2001(eutT)
ECEZ3715
ECSECs_3321(eutT)
ECFECH74115_3680
ETWECSP_3397
ELXCDCO157_3086
EOIECO111_3179(eutT)
EOJECO26_3502(eutT)
EOHECO103_2968(eutT)
ECOOECRM13514_3275
ECOHECRM13516_3136
ESLO3K_07155
ESOO3O_18495
ESMO3M_07200
ECKEC55989_2739(eutT)
ECGE2348C_2693(eutT)
EOKG2583_2981(eutT)
ELRECO55CA74_14755
ELHETEC_2563
ECWEcE24377A_2736(eutT)
EUNUMNK88_3053
ECPECP_2471
ENAECNA114_2525
ECOSEC958_2775(eutT)
ECVAPECO1_4098(eutT)
ECOAAPECO78_15990
ECXEcHS_A2588(eutT)
ECMEcSMS35_2605(eutT)
ECYECSE_2740
ECRECIAI1_2507(eutT)
ECQECED1_2892(eutT)
EUMECUMN_2771(eutT)
ECTECIAI39_2596(eutT)
EOCCE10_2833(eutT)
EBRECB_02350(eutT)
EBLECD_02350(eutT)
EBEB21_02312(eutT)
EBDECBD_1231
ECIUTI89_C2783(eutT)
EIHECOK1_2765(eutT)
ECZECS88_2638(eutT)
ECCc2984
ELOEC042_2658(eutT)
ELNNRG857_12270
ESEECSF_2311
ECLEcolC_1218
EKOEKO11_1279
EKFKO11_10565(eutT)
EABECABU_c27690(eutT)
EDHEcDH1_1211
EDJECDH1ME8569_2384(eutT)
ELUUM146_04380
ELWECW_m2678(eutT)
ELLWFL_13115(eutT)
ELCi14_2781
ELDi02_2781
ELPP12B_c2561(eutT)
ELFLF82_0596(eutT)
ECOLLY180_12600
ECOIECOPMV1_02650
ECOJP423_13560
EFEEFER_0720(eutT)
EALEAKF1_ch3548
EMAC1192_23185
ESZFEM44_02305(eutT)
STYSTY2703
STTt0392
SEXSTBHUCCB_4270
SENTTY21A_02020
STMSTM2467(eutT)
SEOSTM14_3025(eutT)
SEVSTMMW_24861
SEYSL1344_2430(eutT)
SEMSTMDT12_C24860
SEJSTMUK_2499(eutT)
SEBSTM474_2570(eutT)
SEFUMN798_2662
SETUSTU288_08705
SETCCFSAN001921_04430
SENRSTMDT2_24301
SENDDT104_25201
SENICY43_13190
SEENSE451236_18560
SPTSPA0401(eutT)
SEKSSPA0375
SPQSPAB_00485
SEISPC_1193(eutT)
SECSCH_2463(eutT)
SEHSeHA_C2727(eutT)
SHBSU5_03068
SENHCFSAN002069_19425
SEEHSEEH1578_21655
SEESNSL254_A2660(eutT)
SENNSN31241_35720
SEWSeSA_A2701(eutT)
SEASeAg_B2612(eutT)
SENSQ786_12195
SEDSeD_A2834
SEGSG2498(eutT)
SELSPUL_0413(eutT)
SEGASPUCDC_0413(eutT)
SETSEN2447(eutT)
SENAAU38_12415
SENOAU37_12425
SENVAU39_12425
SENQAU40_13925
SENLIY59_12755
SENJCFSAN001992_21245
SEECCFSAN002050_19285
SEEBSEEB0189_007225
SEEPI137_01870
SENBBN855_25530
SENEIA1_12320
SENCSEET0819_19790
SESSARI_00417
SALZEOS98_06630(eutT)
SSNSSON_2539
SBOSBO_2474
SBCSbBS512_E2825(eutT)
SHQA0259_15990
KPNKPN_02793(eutT)
KPUKP1_4043(eutT)
KPMKPHS_38630
KPPA79E_1307
KPHKPNIH24_09350
KPZKPNIH27_18480
KPVKPNIH29_19330
KPWKPNIH30_19530
KPYKPNIH31_18735
KPGKPNIH32_19860
KPCKPNIH10_18855
KPQKPR0928_18875
KPTVK055_4718
KPOKPN2242_17030
KPJN559_1461
KPID364_14230
KPAKPNJ1_01542
KPSKPNJ2_01513
KPXPMK1_00290
KPBFH42_10085
KPNEKU54_007065
KPNULI86_07070
KPNKBN49_4004(eutT)
KVAKvar_1262
KPEKPK_1344(eutT)
KPKA593_04225
KVDKR75_01525
KVQSP68_08045
KOXKOX_27010
KOEA225_4310
KOYJ415_10620
KOMHR38_25165
KOKKONIH1_21245
KOCAB185_15085
KQUAVR78_23555
KQVB8P98_07475
KLLBJF97_21205
KLWDA718_07755(eutT)
KARLGL98_06710(eutT)
KGRJJJ10_07535(eutT)
CROROD_24071(eutT)
CKOCKO_00336
CFDCFNIH1_23700
CBRAA6J81_24065
CWECO701_05605
CYOCD187_07030
CPOTFOB25_18195(eutT)
CFQC2U38_18030
CSEDJY391_06750(eutT)
CAMAF384_13580
CAFAL524_09815
CIFAL515_16780
CFARCI104_18290
CIRC2U53_28595
CIEAN232_11425
CPARCUC49_12610
CTELGBC03_11710(eutT)
CITZE4Z61_23500(eutT)
CARSE1B03_19255(eutT)
PGELG71_11865
ESCEntcl_1308
KLEAO703_15325
BUFD8682_25600(eutT)
BFTMNO13_14550(eutT)
EBFD782_1204
YINCH53_2509
MMKMU9_1036
HAVAT03_09345
OPODSM2777_09435
PGBH744_2c2289
PCQPcP3B5_53410
EMODM558_10170(eutT)
MAQMaqu_1230
FESHER31_01595(eutT)
OAIOLEAN_C11290(eutT)
SEDSAAY24_03050
IODEJO50_14185(eutT)
DEKDSLASN_11370 DSLASN_11650
LMOlmo1181
LMNLM5578_1254
LMYLM5923_1207
LMTLMRG_00627
LMOCLMOSLCC5850_1171(eutT)
LMOEBN418_1385
LMOBBN419_1383
LMODLMON_1174
LMOWAX10_14410
LMOQLM6179_1488
LMRLMR479A_1202
LMOMIJ09_04430
LMFLMOf2365_1191
LMCLm4b_01186
LMOGBN389_12000(eutT)
LMPMUO_06100
LMOLLMOL312_1169(eutT)
LMOJLM220_18875
LMOZLM1816_17890
LMOXAX24_03290
LMHLMHCC_1469
LMQLMM7_1187(eutT)
LMLlmo4a_1164(eutT)
LMGLMKG_01750
LMSLMLG_1080
LMJLMOG_00545
LMWLMOSLCC2755_1174(eutT)
LMXLMOSLCC2372_1178(eutT)
LMZLMOSLCC2482_1221(eutT)
LMONLMOSLCC2376_1133(eutT)
LMOSLMOSLCC7179_1149(eutT)
LMOOLMOSLCC2378_1188(eutT)
LMOYLMOSLCC2479_1178(eutT)
LMOTLMOSLCC2540_1160(eutT)
LMOALMOATCC19117_1182(eutT)
LMOKCQ02_06070
LMVY193_09830
LINlin1145
LWElwe1139
LSGlse_1060(eutT)
LIVLIV_1113
LIIJL52_05900
LIWAX25_06005
LIAJL58_06025
LIOJL53_06555
LMARLAX80_005485
BLRBRLA_c026750
BRWGOP56_05905
PLVERIC2_c11030(eutT)
PIHUB51_11220
SMENSAMEA4412692_0346
VCPH9L18_11670
VHYG7082_08990
CMLBN424_443(eutT)
CPECPE0904
CPFCPF_0897(eutT)
CTCCTC_02171
CTETBN906_02358
CSQCSCA_1617
CACECACET_c04040(eutT)
CFMBJL90_07705
CARGRSJ17_13565
CDRKB9W14_11215
CGASJ1C67_01530
CLOSDMR38_16235
CCAAKQH81_10405
AMTAmet_0261
AOEClos_0803
GFEGferi_15890
HHWNCTC503_00605
CRSFQB35_10050
PBIFKXZ80_05250
FPLAA4U99_02275 A4U99_13280
CLEClole_4086
CEWEKH84_01685
BYLA4V09_06245
BLAUDQQ01_02455
BPROPMF13cell1_04114
BLIQINP51_02475
CPYCphy_2640
ACELacsn021_25440
CDFCD630_19190(eutT)
PDCCDIF630_02123(eutT)
CDCCD196_1794(eutT)
CDLCDR20291_1840(eutT)
PDFCD630DERM_19190(eutT)
CSTCLOST_0253(eutT)
DSYDSY4964
DHDDhaf_4863
DRMDred_1300
FWADCMF_11560
TJRTherJR_0038
CBARPATL70BA_2496
IBUIB211_02636c
AMIJEQM06_11365
AMICAmi3637_00930 Ami3637_09580
ABUTAmi103574_14565
TPZTph_c06990
HPKHprae_0283
XYLET495_08685
ARUBJ5A65_03055
TESBW730_08055
TEZBKM78_13765
TDFH9L22_02590
TLATLA_TLA_02773
SROSros_3359
ATMANT_07250(eutT)
TAZTREAZ_1560
BHYBHWA1_00534(eutT)
BHDBHYOB78_00335
BIPBint_1606(eutT)
BHPBHAMNSH16_00415
FNUFN0085
FNCHMPREF0946_01797
FNTHMPREF0405_01530
FUSHMPREF0409_01867
FNEFSDG_02310
FHWRN87_01540
FPDCTM68_02825
FVAFV113G1_32200
FPEIC4N17_07415
FCII6I83_01590
LBALebu_0074
LHFJCM16775_2444
LHGJMUB5056_0038
STRSterm_1045
TAITaci_0082
SBRSY1_11290
CPORBED41_04160
FLTSv326_1325
 » show all
Reference
1  [PMID:10894741]
  Authors
Fonseca MV, Escalante-Semerena JC
  Title
Reduction of Cob(III)alamin to Cob(II)alamin in Salmonella enterica serovar typhimurium LT2.
  Journal
J Bacteriol 182:4304-9 (2000)
DOI:10.1128/JB.182.15.4304-4309.2000
Reference
2  [PMID:15516577]
  Authors
Sheppard DE, Penrod JT, Bobik T, Kofoid E, Roth JR.
  Title
Evidence that a B12-adenosyl transferase is encoded within the ethanolamine operon of Salmonella enterica.
  Journal
J Bacteriol 186:7635-44 (2004)
DOI:10.1128/JB.186.22.7635-7644.2004
Reference
3  [PMID:16636051]
  Authors
Buan NR, Escalante-Semerena JC.
  Title
Purification and initial biochemical characterization of ATP:Cob(I)alamin adenosyltransferase (EutT) enzyme of Salmonella enterica.
  Journal
J Biol Chem 281:16971-16977 (2006)
DOI:10.1074/jbc.M603069200
Reference
4  [PMID:19933577]
  Authors
Mera PE, Escalante-Semerena JC
  Title
Dihydroflavin-driven adenosylation of 4-coordinate Co(II) corrinoids: are cobalamin reductases enzymes or electron transfer proteins?
  Journal
J Biol Chem 285:2911-7 (2010)
DOI:10.1074/jbc.M109.059485
Reference
5  [PMID:24336938]
  Authors
Moore TC, Mera PE, Escalante-Semerena JC.
  Title
the Eutt enzyme of Salmonella enterica is a unique ATP:Cob(I)alamin adenosyltransferase metalloprotein that requires ferrous ions for maximal activity.
  Journal
J Bacteriol 196:903-10 (2014)
DOI:10.1128/JB.01304-13
Other DBs
ExplorEnz - The Enzyme Database: 2.5.1.154
IUBMB Enzyme Nomenclature: 2.5.1.154
ExPASy - ENZYME nomenclature database: 2.5.1.154
BRENDA, the Enzyme Database: 2.5.1.154

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