KEGG   ENZYME: 4.1.99.26
Entry
EC 4.1.99.26                Enzyme                                 

Name
3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one synthase;
mftC (gene name)
Class
Lyases;
Carbon-carbon lyases;
Other carbon-carbon lyases
Sysname
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one lyase (C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol-forming)
Reaction(IUBMB)
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + 5'-deoxyadenosine + L-methionine + A = C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol + S-adenosyl-L-methionine + AH2 [RN:R12750]
Reaction(KEGG)
R12750
Substrate
C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one [CPD:C22365];
5'-deoxyadenosine [CPD:C05198];
L-methionine [CPD:C00073];
A [CPD:C00028]
Product
C-terminal [mycofactocin precursor peptide]-glycyl-L-valyl-4-[2-aminoethenyl]phenol [CPD:C22345];
S-adenosyl-L-methionine [CPD:C00019];
AH2 [CPD:C00030]
Comment
This is a bifunctional radical AdoMet (radical SAM) enzyme that catalyses the first two steps in the biosynthesis of the enzyme cofactor mycofactocin. Activity requires the presence of the MftB chaperone. The reaction occurs in the right-to-left direction. The other activity of the enzyme is EC 1.3.98.7, [mycofactocin precursor peptide]-tyrosine decarboxylase.
History
EC 4.1.99.26 created 2021
Orthology
K24696  [mycofactocin precursor peptide]-tyrosine decarboxylase / 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one synthase
Genes
THIP: N838_10830
URU: DSM104443_01508(mftC)
UPL: DSM104440_02432(moaA_2) DSM104440_02434(mftC)
GUR: Gura_3559
GEB: GM18_3219
GPI: GPICK_06635
DLI: dnl_37460(mftC)
SPAP: H3Z74_12905
DEX: HWD60_01690(mftC)
DVN: HQ394_08780(mftC)
ECEC: NCTC12421_02257(moaA)
DAE: Dtox_4272
PTH: PTH_0594
MTU: Rv0693
MTV: RVBD_0693
MTC: MT0720
MRA: MRA_0701(pqqE)
MTUR: CFBS_0729(pqqE)
MTO: MTCTRI2_0709(pqqE)
MTD: UDA_0693(pqqE)
MTN: ERDMAN_0765(pqqE)
MTUE: J114_03700
MTUL: TBHG_00688
MTUT: HKBT1_0729(pqqE)
MTUU: HKBT2_0730(pqqE)
MTQ: HKBS1_0729(pqqE)
MBO: BQ2027_MB0712(pqqE)
MBB: BCG_0742(pqqE)
MBT: JTY_0712(pqqE)
MBM: BCGMEX_0713(pqqE)
MBX: BCGT_0485
MAF: MAF_07020(pqqE)
MMIC: RN08_0773
MCE: MCAN_06941(pqqE)
MCQ: BN44_10763(pqqE)
MCV: BN43_20125(pqqE)
MCX: BN42_20448(pqqE)
MCZ: BN45_10793(pqqE)
MPA: MAP_4153(pqqE)
MAO: MAP4_4279
MAVI: RC58_21255
MAVU: RE97_21305
MAV: MAV_4478
MIT: OCO_43690
MIA: OCU_43450
MID: MIP_06630
MYO: OEM_43920
MIR: OCQ_44800
MMAL: CKJ54_20795(mftC)
MLP: MLM_3634
MUL: MUL_0773(pqqE)
MMC: Mmcs_1001
MKM: Mkms_1018
MJL: Mjls_1028
MMI: MMAR_1021(pqqE)
MMAE: MMARE11_09740(pqqE)
MMM: W7S_22025
MLI: MULP_01148(pqqE)
MHAD: B586_18795
MSHG: MSG_00882(mftC)
MFJ: MFLOJ_25800(mftC)
MSTO: MSTO_29440(mftC)
MGRO: FZ046_11350(mftC)
MPAG: C0J29_05580(mftC)
MGOR: H0P51_05075(mftC)
MCOO: MCOO_41760
MBAI: MB901379_00882(albA)
MSEO: MSEO_48250(pqqE)
MSG: MSMEI_1388(pqqE)
MVA: Mvan_1296
MGI: Mflv_5060
MPHL: MPHLCCUG_01293(albA)
MVQ: MYVA_1101
MTHN: 4412656_00903(moaA_1)
MHAS: MHAS_00222(mftC)
MAUU: NCTC10437_01079(moaA_1)
MMAG: MMAD_11150
MMOR: MMOR_54180
MAIC: MAIC_45870
MALV: MALV_24330
MARZ: MARA_27880
MGAD: MGAD_28140
MHEV: MHEL_11880
MSAR: MSAR_25550
MANY: MANY_49630
MAUB: MAUB_22120
MPOF: MPOR_15780
MAB: MAB_3835c
MABB: MASS_3846
MCHE: BB28_19635
MSTE: MSTE_03984
MSAL: DSM43276_03628(albA_1)
MJD: JDM601_3348(pqqE)
MTER: 4434518_03335(pqqE)
MMIN: MMIN_10500
MHIB: MHIB_27760
NFR: ERS450000_00607(moaA_1) ERS450000_01864(moaA_2)
NAH: F5544_40635(mftC)
NAD: NCTC11293_06440(moaA_2)
RER: RER_17990
REY: O5Y_08630
ROP: ROP_61300
REQ: REQ_36270
RHB: NY08_1952
RFA: A3L23_00297(mftC)
RHS: A3Q41_03117(mftC)
RRZ: CS378_08060(mftC)
RHU: A3Q40_00412(mftC)
RQI: C1M55_09105(mftC)
RRT: 4535765_03565(moaA_2)
RBY: CEJ39_19670(mftC)
RCR: NCTC10994_03687(moaA_1)
RTM: G4H71_16285(mftC)
GBR: Gbro_3778
GOR: KTR9_3737
GOC: CXX93_06955(mftC)
GIT: C6V83_16215(mftC)
GRU: GCWB2_19180(albA)
GOM: D7316_04926(mftC)
GAV: C5O27_08960(mftC)
GOD: GKZ92_18110(mftC)
DIT: C3V38_01380(mftC)
DIZ: CT688_11595(mftC)
TOY: FO059_05810(mftC)
SHY: SHJG_2443
MSED: E3O41_00690(mftC)
MSF: IT882_01150(mftC)
HUM: DVJ78_13615(mftC)
HEA: HL652_05825(mftC)
CHRE: IE160_03000(mftC)
JLI: EXU32_11045(mftC)
PHW: G7075_01305(mftC)
NDP: E2C04_03200(mftC)
PSIM: KR76_24775
AEZ: C3E78_15430(mftC)
AEB: C6I20_03055(mftC)
AEF: GEV26_02910(mftC)
NGV: CDO52_16170(mftC)
TCU: Tcur_2362
ACTW: F7P10_02075(mftC)
FAL: FRAAL3572(pqqE)
NML: Namu_0775
GOB: Gobs_4936
MMAR: MODMU_5392
SEN: SACE_2389(pqqE)
SACG: FDZ84_29565(mftC) FDZ84_34715(mftC)
AMQ: AMETH_4935(pqqE)
AMYC: CU254_14360(mftC)
PDX: Psed_5681
PSEA: WY02_13545
PSEH: XF36_00070
PAUT: Pdca_61410
ALO: CRK56114
ASE: ACPL_6044(pqqE)
ACTS: ACWT_5912
EKE: EK0264_07230(mftC)
RXY: Rxyl_3154
TRO: trd_A0840
STI: Sthe_2856
 » show all
Reference
1  [PMID:21223593]
  Authors
Haft DH.
  Title
Bioinformatic evidence for a widely distributed, ribosomally produced electron carrier precursor, its maturation proteins, and its nicotinoprotein redox partners.
  Journal
BMC Genomics 12:21 (2011)
DOI:10.1186/1471-2164-12-21
  Sequence
[mtu:Rv0693]
Reference
2  [PMID:27158836]
  Authors
Bruender NA, Bandarian V
  Title
The Radical S-Adenosyl-l-methionine Enzyme MftC Catalyzes an Oxidative Decarboxylation of the C-Terminus of the MftA Peptide.
  Journal
Biochemistry 55:2813-6 (2016)
DOI:10.1021/acs.biochem.6b00355
Reference
3  [PMID:28634235]
  Authors
Khaliullin B, Ayikpoe R, Tuttle M, Latham JA
  Title
Mechanistic elucidation of the mycofactocin-biosynthetic radical S-adenosylmethionine protein, MftC.
  Journal
J Biol Chem 292:13022-13033 (2017)
DOI:10.1074/jbc.M117.795682
  Sequence
[mul:MUL_0773]
Reference
4  [PMID:30628436]
  Authors
Ayikpoe R, Ngendahimana T, Langton M, Bonitatibus S, Walker LM, Eaton SS, Eaton GR, Pandelia ME, Elliott SJ, Latham JA.
  Title
Spectroscopic and Electrochemical Characterization of the Mycofactocin Biosynthetic Protein, MftC, Provides Insight into Its Redox Flipping Mechanism.
  Journal
Biochemistry 58:940-950 (2019)
DOI:10.1021/acs.biochem.8b01082
  Sequence
[mul:MUL_0773]
Other DBs
ExplorEnz - The Enzyme Database: 4.1.99.26
IUBMB Enzyme Nomenclature: 4.1.99.26
ExPASy - ENZYME nomenclature database: 4.1.99.26
BRENDA, the Enzyme Database: 4.1.99.26

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