ID   MNMG_CLOPE              Reviewed;         630 AA.
AC   Q8XH31;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 101.
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}; OrderedLocusNames=CPE2654;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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; BA000016; BAB82360.1; -; Genomic_DNA.
DR   RefSeq; WP_011011003.1; NC_003366.1.
DR   AlphaFoldDB; Q8XH31; -.
DR   SMR; Q8XH31; -.
DR   STRING; 195102.gene:10491998; -.
DR   EnsemblBacteria; BAB82360; BAB82360; BAB82360.
DR   KEGG; cpe:CPE2654; -.
DR   HOGENOM; CLU_007831_2_2_9; -.
DR   OMA; FRPGYAI; -.
DR   Proteomes; UP000000818; 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..630
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000117088"
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   630 AA;  70625 MW;  159131D51F0DCF2C CRC64;
     MRYNAGSYDI VVIGAGHAGC EAGLAAARMG CKTLVCTLTL DSVAMMPCNP NIGGTAKGHL
     VREIDALGGE MGVNIDHTFI QSKMLNTSKG PAVHSLRAQA DKKKYQERMK KVLETQENLH
     LRQLEVVSVE VEDGKVKGVL TKNGAFFECK AVIMTSGTYL QSRIIIGDVS YSQGPNGLSN
     ANELSKSLID LGIDLRRFKT GTPARINKRS VDFSKMIEQP GDEEIIPFSF ISGNIDRDQV
     SCWLTYTNEE THKVIQENIH RSPMYNGSIK GVGPRYCPSI EDKVMRFQDK DRHQIFIEPE
     GDDTEEMYVG GMSSSLPEDV QVQMIKTVPG LENAEIMRTA YAIEYDCIDP TQLKASLEFK
     NIDGFFSAGQ INGSSGYEEA GAQGIVAGIN AALKVQGKDP MILTRSDGYV GVLIDDLITK
     GTNEPYRMMT SRAEYRLLLR QDNADFRLTE IGHNVGLVTE ERWNKFKERK QNLERELERL
     KELQITNKTE NNEKIVELGS TELKKPIRMY ELIKRPELDY FSLACLDPER PDLPKDIGDQ
     INIIARYEGY IQTQLEQVAQ FKKFEKKVLP EDLDYNDVNS LRIEAIQKLN KIRPLNIGQA
     SRISGVSPAD ISVLLIFLEH YRKTGKNTDN