ID   MNMG_CARRP              Reviewed;         500 AA.
AC   Q05FY8;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG;
DE   AltName: Full=Glucose-inhibited division protein A;
GN   Name=mnmG; Synonyms=gidA; OrderedLocusNames=CRP_002;
OS   Carsonella ruddii (strain PV).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Zymobacter group; Candidatus Carsonella.
OX   NCBI_TaxID=387662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PV;
RX   PubMed=17038615; DOI=10.1126/science.1134196;
RA   Nakabachi A., Yamashita A., Toh H., Ishikawa H., Dunbar H.E., Moran N.A.,
RA   Hattori M.;
RT   "The 160-kilobase genome of the bacterial endosymbiont Carsonella.";
RL   Science 314:267-267(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:0000250}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MnmG family. {ECO:0000305}.
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DR   EMBL; AP009180; BAF35033.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q05FY8; -.
DR   SMR; Q05FY8; -.
DR   STRING; 387662.CRP_002; -.
DR   EnsemblBacteria; BAF35033; BAF35033; CRP_002.
DR   KEGG; crp:CRP_002; -.
DR   HOGENOM; CLU_007831_0_0_6; -.
DR   OMA; FRPGYAI; -.
DR   Proteomes; UP000000777; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 2.
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; 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   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..500
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345251"
FT   BINDING         10..15
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         262..276
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   500 AA;  58315 MW;  EF32071715518C42 CRC64;
     MNIFNIIIIG AGHSGIEAAI SASKICNKIK IITSNLENLG IMSCNPSIGG IGKSHLVKEL
     ELFGGIMPEA SDYSRIHSKL LNYKKGESVH SLRYQIDRIL YKNYILKILF LKKNILIEQN
     EINKIIRFKK KILIFNKLKF FNIAKIIIVC AGTFINSKIY IGKNIKALNK AEKKSISYSF
     KKINLFISKL KTGTPPRLDL NYLNYKKLSV QYSDYTISYG KNFNFNNNVK CFITNTDNKI
     NNFIKKNIKN SSLFNLKFKS IGPRYCPSIE DKIFKFPNNK NHQIFLEPES YFSKEIYVNG
     LSNSLSYNIQ KKLIKKILGI KKSYIIRYAY NIQYDYFDPR CLKISLNIKF ANNIFLAGQI
     NGTTGYEEAS SQGFVAGINS ARKILKLPLW KPKKWNSYIG VLLYDLTNFG IQEPYRIFTS
     KSDNRLFLRF DNAIFRLINI SYYLGCLPIV KFKYYNSLIY KFYKNLINIR KIKLFDNFYL
     FKLIIIMSKY YGYIKKKYFK