ID   MNMG_CLOBL              Reviewed;         625 AA.
AC   A7GJN8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG {ECO:0000255|HAMAP-Rule:MF_00129};
DE   AltName: Full=Glucose-inhibited division protein A {ECO:0000255|HAMAP-Rule:MF_00129};
GN   Name=mnmG {ECO:0000255|HAMAP-Rule:MF_00129};
GN   Synonyms=gidA {ECO:0000255|HAMAP-Rule:MF_00129};
GN   OrderedLocusNames=CLI_3887;
OS   Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Langeland / NCTC 10281 / Type F;
RA   Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA   Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NAD-binding protein involved in the addition of a
CC       carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of
CC       certain tRNAs, forming tRNA-cmnm(5)s(2)U34. {ECO:0000255|HAMAP-
CC       Rule:MF_00129}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00129};
CC   -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00129}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00129}.
CC   -!- SIMILARITY: Belongs to the MnmG family. {ECO:0000255|HAMAP-
CC       Rule:MF_00129}.
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DR   EMBL; CP000728; ABS40537.1; -; Genomic_DNA.
DR   RefSeq; WP_012101231.1; NC_009699.1.
DR   AlphaFoldDB; A7GJN8; -.
DR   SMR; A7GJN8; -.
DR   EnsemblBacteria; ABS40537; ABS40537; CLI_3887.
DR   KEGG; cbf:CLI_3887; -.
DR   HOGENOM; CLU_007831_2_2_9; -.
DR   OMA; FRPGYAI; -.
DR   Proteomes; UP000002410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR   Gene3D; 1.10.150.570; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   HAMAP; MF_00129; MnmG_GidA; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR004416; MnmG.
DR   InterPro; IPR002218; MnmG-rel.
DR   InterPro; IPR020595; MnmG-rel_CS.
DR   InterPro; IPR026904; MnmG_C.
DR   InterPro; IPR044920; MnmG_C_subdom.
DR   InterPro; IPR040131; MnmG_N.
DR   PANTHER; PTHR11806; PTHR11806; 1.
DR   PANTHER; PTHR11806:SF0; PTHR11806:SF0; 1.
DR   Pfam; PF01134; GIDA; 1.
DR   Pfam; PF13932; GIDA_C; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR00136; gidA; 1.
DR   PROSITE; PS01280; GIDA_1; 1.
DR   PROSITE; PS01281; GIDA_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; NAD; tRNA processing.
FT   CHAIN           1..625
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_1000016583"
FT   BINDING         14..19
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         273..287
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   625 AA;  70572 MW;  09D9D344221D8AEA CRC64;
     MKYLAGDFDV VVIGAGHAGC EAALASARMG CKTLICTMNL DSIALMACNP NIGGTAKGHL
     VREIDALGGE MGINIDHTFI QSRMLNTSKG PAVHSLRAQA DKKRYSERMK HLLEKEDNVV
     LRQLEVIEID VEDNEVKGVL TKNGAYFTTK AIILCTGTYL KGKIIIGDII YSSGPSGLYP
     ANDLSQSLLD LGINLRRFKT GTPARINKRS VDFSKMIEQP GDEKIVPFSF IHNKLDKDQI
     SCYLTYTSEE THKIIHQNIH RSPLYNGSIE GVGPRYCPSI EDKIVRFPDK DKHQIFIEPE
     GENTEELYVG GMSSSLPEDV QIKMYRSVPG LENAEILRTA YAIEYDCIDP QQLDLTLEFK
     NINGLYGAGQ FNGSSGYEEA AAQGLIAGIN AVLKIKEKNP LILKRSDAYI GVLIDDLVTK
     GTNEPYRMMT SRAEYRLLLR QDNADLRLTE LGYKVGLVKE DRYNKFLNRK KNVENEIERL
     RNMQITGKRE INEFLLEKGS TELKKPISLY ELIKRPELDY FKVEPLDDKR PSLSDDEKEE
     INIIAKYEGY INKQLEQVEQ FKKYEDRLIP KSINYLDIKG LRLEAIQKLE KIKPINIGQA
     SRISGVSPAD ISVLLIYMER KNREN