ID   MNMG_CLOTE              Reviewed;         623 AA.
AC   Q899S1;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=CTC_00099;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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; AE015927; AAO34751.1; -; Genomic_DNA.
DR   RefSeq; WP_011098423.1; NC_004557.1.
DR   AlphaFoldDB; Q899S1; -.
DR   SMR; Q899S1; -.
DR   STRING; 212717.CTC_00099; -.
DR   EnsemblBacteria; AAO34751; AAO34751; CTC_00099.
DR   GeneID; 64180679; -.
DR   KEGG; ctc:CTC_00099; -.
DR   HOGENOM; CLU_007831_2_2_9; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000001412; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; NAD; Reference proteome; tRNA processing.
FT   CHAIN           1..623
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000117089"
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   623 AA;  69943 MW;  C9F03133AFAD667C CRC64;
     MKYYAGDYDV VVVGAGHAGC EAALAAARIG CKVLICTISL DSVALMPCNP NIGGTAKGHL
     VREIDALGGE MGVNIDNTFI QSRMLNTSKG PAVHSLRAQA DKSRYSNRMK YILENEENVT
     LKQIEVISID IENGKVKGIL TKNGAYYNAK TVVLATGTYL NARIIIGEVA YSGGPNGLFP
     AKELTKNLMD LGISIRRFKT GTPARVNKKT IDFSKMIEQP GDEKIVPFSF LTDKLEREQV
     SCYLTYTNEN THEVIRKNLH RSPMFNGSIE GVGARYCPSI EDKVNRFPDK NKHQVFIEPE
     GEYTNEMYVS GLSSSLPEEI QVAMYRTVPG LENVEFLRTA YAIEYDCIDP QELKLSLESK
     NIEGLFSGGQ INGSSGYEEA AAQGLIAGIN AAMKVKEKDP LLLTRSDGYI GVLIDDLVTK
     GTNEPYRMMT SRSEYRLLLR QGNADLRLTQ KGYDVGLVSE ERYKRYINRR ESIKSEIERI
     KNVQITNKKE VNEFLLSLNS SELKKPISLY ELIKRPELDY YKVEQLDKGR INLPEDVQEE
     VNTTAKYEGY IEKQLEQVNQ FKKFENKLLP NDIDYSKVYG LRIESVQKLS KIRPMNIGQA
     SRISGVSPAD ISVLLIYLEH KYK