MFTC_MYCTO
ID MFTC_MYCTO Reviewed; 391 AA.
AC P9WJ78; L0T7F8; P95039; Q7D9E9;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Mycofactocin maturase MftC;
DE AltName: Full=[Mycofactocin precursor peptide]-pyrrolidinone derivative synthase;
DE EC=4.1.99.26 {ECO:0000250|UniProtKB:A0PM49};
DE AltName: Full=[Mycofactocin precursor peptide]-tyrosine decarboxylase;
DE EC=1.3.98.7 {ECO:0000250|UniProtKB:A0PM49};
GN Name=mftC; OrderedLocusNames=MT0720;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Radical S-adenosylmethionine (SAM) enzyme responsible for the
CC first step of the biosynthesis of the enzyme cofactor mycofactocin
CC (MFT). Catalyzes two reactions at the C-terminus of the mycofactocin
CC precursor (the MftA peptide). The first one is the oxidative
CC decarboxylation of the C-terminal L-tyrosine of MftA, forming an
CC unsaturated tyramine moiety. The second reaction is the cross-linking
CC of the tyramine with the penultimate L-valine residue, forming a five-
CC membered lactam ring. Its activity requires the presence of the MftB
CC chaperone. {ECO:0000250|UniProtKB:A0PM49}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[mycofactocin precursor peptide]-C-terminal glycyl-L-valyl-L-
CC tyrosine + S-adenosyl-L-methionine = 5'-deoxyadenosine +
CC [mycofactocin precursor peptide]-C-terminal glycyl-N-{[2-(4-
CC hydroxyphenyl)ethenyl]-3-methylbutanamide} + CO2 + L-methionine;
CC Xref=Rhea:RHEA:65492, Rhea:RHEA-COMP:16815, Rhea:RHEA-COMP:16816,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:17319, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:156515, ChEBI:CHEBI:156517;
CC EC=1.3.98.7; Evidence={ECO:0000250|UniProtKB:A0PM49};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[mycofactocin precursor peptide]-C-terminal glycyl-N-{[2-(4-
CC hydroxyphenyl)ethenyl]-3-methylbutanamide} + AH2 + S-adenosyl-L-
CC methionine = 5'-deoxyadenosine + [mycofactocin precursor peptide]-C-
CC terminal glycyl-N-{5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-
CC oxopyrrolidin-3-yl}acetamide + A + H(+) + L-methionine;
CC Xref=Rhea:RHEA:65500, Rhea:RHEA-COMP:16816, Rhea:RHEA-COMP:16818,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:156517, ChEBI:CHEBI:156518; EC=4.1.99.26;
CC Evidence={ECO:0000250|UniProtKB:A0PM49};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:A0PM49};
CC Note=Binds 3 [4Fe-4S] clusters. One cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine. All three [Fe-S]
CC clusters are required for MftC modification of MftA.
CC {ECO:0000250|UniProtKB:A0PM49};
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. {ECO:0000305}.
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DR EMBL; AE000516; AAK44949.1; -; Genomic_DNA.
DR PIR; H70640; H70640.
DR RefSeq; WP_003403490.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WJ78; -.
DR SMR; P9WJ78; -.
DR EnsemblBacteria; AAK44949; AAK44949; MT0720.
DR KEGG; mtc:MT0720; -.
DR PATRIC; fig|83331.31.peg.770; -.
DR HOGENOM; CLU_009273_4_3_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR023885; 4Fe4S-binding_SPASM_dom.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR034391; Cmo-like_SPASM_containing.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR023913; MftC.
DR InterPro; IPR017200; PqqE-like.
DR InterPro; IPR007197; rSAM.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF13186; SPASM; 1.
DR PIRSF; PIRSF037420; PQQ_syn_pqqE; 1.
DR SFLD; SFLDG01387; BtrN-like_SPASM_domain_contain; 1.
DR SFLD; SFLDF00316; C-terminal_tyrosine_decarboxyl; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR03962; mycofact_rSAM; 1.
DR TIGRFAMs; TIGR04085; rSAM_more_4Fe4S; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; Oxidoreductase;
KW S-adenosyl-L-methionine.
FT CHAIN 1..391
FT /note="Mycofactocin maturase MftC"
FT /id="PRO_0000427877"
FT DOMAIN 16..232
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT REGION 340..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 30
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:A0PM49"
FT BINDING 34
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:A0PM49"
FT BINDING 37
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:A0PM49"
FT BINDING 251
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0PM49"
FT BINDING 258
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0PM49"
FT BINDING 269
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0PM49"
FT BINDING 310
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:A0PM49"
FT BINDING 313
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:A0PM49"
FT BINDING 319
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:A0PM49"
FT BINDING 323
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0PM49"
FT BINDING 341
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:A0PM49"
SQ SEQUENCE 391 AA; 42448 MW; CEE338AA1CE6A70A CRC64;
MTSPVPRLIE QFERGLDAPI CLTWELTYAC NLACVHCLSS SGKRDPGELS TRQCKDIIDE
LERMQVFYVN IGGGEPTVRP DFWELVDYAT AHHVGVKFST NGVRITPEVA TRLAATDYVD
VQISLDGATA EVNDAIRGTG SFDMAVRALQ NLAAAGFAGV KISVVITRRN VAQLDEFATL
ASRYGATLRI TRLRPSGRGT DVWADLHPTA DQQVQLYDWL VSKGERVLTG DSFFHLAPLG
QSGALAGLNM CGAGRVVCLI DPVGDVYACP FAIHDHFLAG NVLSDGGFQN VWKNSSLFRE
LREPQSAGAC GSCGHYDSCR GGCMAAKFFT GLPLDGPDPE CVQGHSEPAL ARERHLPRPR
ADHSRGRRVS KPVPLTLSMR PPKRPCNESP V
