ID   MFTD_MYCTO              Reviewed;         396 AA.
AC   P9WND6; L0T788; P95040; Q8VKG1;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Pre-mycofactocin synthase;
DE            Short=PMFT synthase;
DE            EC=1.4.3.26 {ECO:0000250|UniProtKB:A0PM50};
GN   Name=mftD; Synonyms=lldD1; OrderedLocusNames=MT0721;
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: Involved in the biosynthesis of the enzyme cofactor
CC       mycofactocin (MFT). Catalyzes the oxidative deamination of AHDP (3-
CC       amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidin-2-one),
CC       forming an alpha-keto amide moiety on the resulting molecule, which is
CC       called pre-mycofactocin (PMFT). This reaction occurs via a 5-[(4-
CC       hydroxyphenyl)methyl]-3-imino-4,4-dimethylpyrrolidin-2-one
CC       intermediate, which converts to PMFT. The alpha-keto amide moiety is
CC       the redox-active center for the redox activity of mycofactocin.
CC       {ECO:0000250|UniProtKB:A0PM50}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidin-
CC         2-one + H2O + O2 = H2O2 + NH4(+) + pre-mycofactocin;
CC         Xref=Rhea:RHEA:65508, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:150862,
CC         ChEBI:CHEBI:150863; EC=1.4.3.26;
CC         Evidence={ECO:0000250|UniProtKB:A0PM50};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:A0PM50};
CC   -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC       dehydrogenase family. {ECO:0000255|PROSITE-ProRule:PRU00683}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK44950.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK44950.1; ALT_FRAME; Genomic_DNA.
DR   PIR; A70641; A70641.
DR   AlphaFoldDB; P9WND6; -.
DR   SMR; P9WND6; -.
DR   EnsemblBacteria; AAK44950; AAK44950; MT0721.
DR   KEGG; mtc:MT0721; -.
DR   HOGENOM; CLU_020639_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN.
DR   InterPro; IPR000262; FMN-dep_DH.
DR   InterPro; IPR037396; FMN_HAD.
DR   InterPro; IPR023989; MftD.
DR   Pfam; PF01070; FMN_dh; 1.
DR   PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1.
DR   TIGRFAMs; TIGR03966; actino_HemFlav; 1.
DR   PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE   3: Inferred from homology;
KW   Flavoprotein; FMN; Oxidoreductase.
FT   CHAIN           1..396
FT                   /note="Pre-mycofactocin synthase"
FT                   /id="PRO_0000427145"
FT   DOMAIN          1..383
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   ACT_SITE        278
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         108
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         128
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         156
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         254
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         309..313
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT   BINDING         332..333
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
SQ   SEQUENCE   396 AA;  42161 MW;  9E9154FC4A55E610 CRC64;
     MAEAWFETVA IAQQRAKRRL PKSVYSSLIA ASEKGITVAD NVAAFSELGF APHVIGATDK
     RDLSTTVMGQ EVSLPVIISP TGVQAVDPGG EVAVARAAAA RGTVMGLSSF ASKPIEEVIA
     ANPKTFFQVY WQGGRDALAE RVERARQAGA VGLVVTTDWT FSHGRDWGSP KIPEEMNLKT
     ILRLSPEAIT RPRWLWKFAK TLRPPDLRVP NQGRRGEPGP PFFAAYGEWM ATPPPTWEDI
     GWLRELWGGP FMLKGVMRVD DAKRAVDAGV SAISVSNHGG NNLDGTPASI RALPAVSAAV
     GDQVEVLLDG GIRRGSDVVK AVALGARAVM IGRAYLWGLA ANGQAGVENV LDILRGGIDS
     ALMGLGHASV HDLSPADILV PTGFIRDLGV PSRRDV