MFTD_MYCUA
ID MFTD_MYCUA Reviewed; 390 AA.
AC A0PM50;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Pre-mycofactocin synthase {ECO:0000305|PubMed:31381312};
DE Short=PMFT synthase {ECO:0000305|PubMed:31381312};
DE EC=1.4.3.26 {ECO:0000269|PubMed:31381312};
GN Name=mftD {ECO:0000303|PubMed:31381312};
GN Synonyms=lldD1 {ECO:0000312|EMBL:ABL03419.1};
GN OrderedLocusNames=MUL_0774 {ECO:0000312|EMBL:ABL03419.1};
OS Mycobacterium ulcerans (strain Agy99).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=362242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Agy99;
RX PubMed=17210928; DOI=10.1101/gr.5942807;
RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT "Reductive evolution and niche adaptation inferred from the genome of
RT Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL Genome Res. 17:192-200(2007).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RC STRAIN=Agy99;
RX PubMed=31381312; DOI=10.1021/jacs.9b06102;
RA Ayikpoe R.S., Latham J.A.;
RT "MftD Catalyzes the Formation of a Biologically Active Redox Center in the
RT Biosynthesis of the Ribosomally Synthesized and Post-translationally
RT Modified Redox Cofactor Mycofactocin.";
RL J. Am. Chem. Soc. 141:13582-13591(2019).
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:0000269|PubMed:31381312}.
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:0000269|PubMed:31381312};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:31381312};
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; CP000325; ABL03419.1; -; Genomic_DNA.
DR RefSeq; WP_011739044.1; NC_008611.1.
DR AlphaFoldDB; A0PM50; -.
DR SMR; A0PM50; -.
DR STRING; 362242.MUL_0774; -.
DR EnsemblBacteria; ABL03419; ABL03419; MUL_0774.
DR KEGG; mul:MUL_0774; -.
DR eggNOG; COG1304; Bacteria.
DR HOGENOM; CLU_020639_0_0_11; -.
DR OMA; AWSWEKI; -.
DR BioCyc; MetaCyc:MON-21116; -.
DR BRENDA; 1.4.3.26; 8016.
DR Proteomes; UP000000765; 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 1: Evidence at protein level;
KW Flavoprotein; FMN; Oxidoreductase.
FT CHAIN 1..390
FT /note="Pre-mycofactocin synthase"
FT /id="PRO_0000452054"
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 390 AA; 41780 MW; 4DC20C6338E4E67F CRC64;
MADEWFETVA IAQQRAKRRL PKSVYSSLIS ASEKGITVAD NVAAFSELGF APHVIGAAEK
RDMSTTVMGQ DISMPVLISP TGVQAVHPDG EVAVARAAAA RGTAMGLSSF ASKTIEDVIA
ANPKIFFQIY WLGGRDAIAE RVERARQAGA VGLIVTTDWT FSHGRDWGSP KIPEQMNLRT
ILRLSPEAIV RPRWLWKFGK TLRPPDLRVP NQGRRGEPGP AFFAAYGEWM GTPPPTWDDI
AWLRELWGGP FMLKGVMRVD DAKRAVDAGV SAISVSNHGG NNLDGTPASI RALPAVAAAV
GDQVEVLLDG GIRRGSDVVK AVALGARAVL VGRAYLWGLA ANGQAGVENV LDILRGGIDS
ALMGLGHSSI HDLRSDDILI PADFVRRLGR
