MFTD_MYCTU
ID MFTD_MYCTU Reviewed; 396 AA.
AC P9WND7; 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 40.
DE RecName: Full=Pre-mycofactocin synthase;
DE Short=PMFT synthase;
DE EC=1.4.3.26 {ECO:0000250|UniProtKB:A0PM50};
GN Name=mftD {ECO:0000303|PubMed:21223593}; Synonyms=lldD1;
GN OrderedLocusNames=Rv0694;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP POSSIBLE FUNCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21223593; DOI=10.1186/1471-2164-12-21;
RA Haft D.H.;
RT "Bioinformatic evidence for a widely distributed, ribosomally produced
RT electron carrier precursor, its maturation proteins, and its
RT nicotinoprotein redox partners.";
RL BMC Genomics 12:21-21(2011).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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}.
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DR EMBL; AL123456; CCP43438.1; -; Genomic_DNA.
DR PIR; A70641; A70641.
DR RefSeq; NP_215208.1; NC_000962.3.
DR RefSeq; WP_003898557.1; NZ_NVQJ01000007.1.
DR AlphaFoldDB; P9WND7; -.
DR SMR; P9WND7; -.
DR STRING; 83332.Rv0694; -.
DR PaxDb; P9WND7; -.
DR DNASU; 888310; -.
DR GeneID; 45424656; -.
DR GeneID; 888310; -.
DR KEGG; mtu:Rv0694; -.
DR TubercuList; Rv0694; -.
DR eggNOG; COG1304; Bacteria.
DR OMA; AWSWEKI; -.
DR PhylomeDB; P9WND7; -.
DR BRENDA; 1.4.3.26; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0019516; P:lactate oxidation; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..396
FT /note="Pre-mycofactocin synthase"
FT /id="PRO_0000390892"
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
