ID   MNMG_CLOD6              Reviewed;         631 AA.
AC   Q181S8;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=CD630_36750;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM180355; CAJ70584.1; -; Genomic_DNA.
DR   RefSeq; WP_009898858.1; NZ_CP010905.2.
DR   RefSeq; YP_001090199.1; NC_009089.1.
DR   AlphaFoldDB; Q181S8; -.
DR   SMR; Q181S8; -.
DR   STRING; 272563.CD630_36750; -.
DR   PRIDE; Q181S8; -.
DR   EnsemblBacteria; CAJ70584; CAJ70584; CD630_36750.
DR   KEGG; cdf:CD630_36750; -.
DR   KEGG; pdc:CDIF630_04005; -.
DR   PATRIC; fig|272563.120.peg.3887; -.
DR   eggNOG; COG0445; Bacteria.
DR   OMA; FRPGYAI; -.
DR   PhylomeDB; Q181S8; -.
DR   BioCyc; PDIF272563:G12WB-3867-MON; -.
DR   Proteomes; UP000001978; 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; Reference proteome; tRNA processing.
FT   CHAIN           1..631
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345260"
FT   BINDING         15..20
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         274..288
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   631 AA;  70731 MW;  2F61AC5BF5D37E94 CRC64;
     MIKFEAGKYD VIVVGAGHAG CEAALATARM GYKTLIITMS LDSIALMPCN PSIGGTGKGQ
     LVKEIDALGG QMGLNIDKTY IQSRMLNTAK GPAVHSLRAQ ADKFKYHEEM KKTLEDEPNL
     DIAMDEVVEI LHEGNVVIGV GTKLGCSFKS KAVILATGVY LNSKIYMGEV AFYEGPNALG
     YAKYLTDSLV ELGLRMRRFK TGTPARVHRD SIDFSVMSLQ EGDEKVTPFS FMNENIEKKQ
     EPCYLTRTTE ETQKVILDNL KRSAMYSGVI ESTGPRYCPS IEDKVVRFSD KTSHQLFIEP
     EGLNTKEMYI QGISTSLPFE VQLDMYKTIK GLENCKIMRP AYAIEYDCVD PTQLKISLEI
     KGVENLFSAG QFNGTSGYEE AAAQGLMAGI NAVRKIEGKE PFVLDRSEAY IGVLLDDLVT
     KGTNEPYRMM TSRAEYRLYL RQDNADMRLT QKGYDIGLVK KDRYERFLNK KAAVEKEFER
     LKNERVTPKE VNSLLEEKGA TPIKVGISLY EFLKRPEVTY ELLEELGKGA GDDVSREVKE
     QCVIITKYEG YIEKQLKQID QFKKLENKKL DEKINYSSIE GLRLEARQKL DDIKPISIGQ
     ASRISGVSPA DISVLLIYLE QIRRTRGGKG E