ID   MNMG_DESHY              Reviewed;         637 AA.
AC   Q24M99;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=DSY5054;
OS   Desulfitobacterium hafniense (strain Y51).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=138119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y51;
RX   PubMed=16513756; DOI=10.1128/jb.188.6.2262-2274.2006;
RA   Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA   Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT   "Complete genome sequence of the dehalorespiring bacterium
RT   Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT   ethenogenes 195.";
RL   J. Bacteriol. 188:2262-2274(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}.
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DR   EMBL; AP008230; BAE86843.1; -; Genomic_DNA.
DR   RefSeq; WP_011462329.1; NC_007907.1.
DR   AlphaFoldDB; Q24M99; -.
DR   SMR; Q24M99; -.
DR   STRING; 138119.DSY5054; -.
DR   EnsemblBacteria; BAE86843; BAE86843; DSY5054.
DR   KEGG; dsy:DSY5054; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_9; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000001946; 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..637
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345262"
FT   BINDING         14..19
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         279..293
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   637 AA;  70439 MW;  4023638683AB0F88 CRC64;
     MEYLAGNYDV IVVGAGHAGC EAALAAARMG GRTLLITLSL DNIAHMDCNP SLGGPAKGHL
     VREIDALGGQ MGITADETSL QVRMLNTGKG PAVHALRIQS DKQAYHLHMR NAILGQENLV
     LHQALVERIK TEDGKVSGVV TRTGAFYAAP NVILTSGTYL RGRIIIGDAM YEGGPNGQQT
     AMNLSGALKE LGLELGRFKT GTPPRIHRRS VDYTKFTVQP GDSVPWRYSF MPTQSMFWGR
     DVDKQIPCWL GYTTPETHQI IQDNIHRAPL YSGKIEGIGP RYCPSIEDKV VRFADRPTHQ
     IFLEPEGWNS DELYVAGLST SMPEEIQYDI IHSIPGLEKA ELLRPGYAIE YDYVKPYQLS
     LSLEVRRIPG LFTAGQLNGT SGYEEAAAQG LLAGINAALR VQGKEPFIVR RSEGYLGVLI
     DDLVNKGVKE PYRLLTSRAE YRLILRQDNA DLRLTPRGRE VGLVKDERWA AFQKKKAAIA
     EINALWRGTT FSPLNEHLAE VLAGVHSAPV HGGISGEELM RRPEITINEI KQLIPQLAEY
     DEEALLEAGI EIKYAGYIEK QLAEIERFAK MEERMIPEEI VYDQIKGLST EGRQRLKEVA
     PANMGQATRI TGVTPADISV LLVYLEQKRR GGQIHAT