ID   MNMG_ENDTX              Reviewed;         597 AA.
AC   B1H0R2;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=TGRD_611;
OS   Endomicrobium trichonymphae.
OC   Bacteria; Elusimicrobia; Endomicrobia; Endomicrobiales; Endomicrobiaceae;
OC   Endomicrobium.
OX   NCBI_TaxID=1408204;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18391199; DOI=10.1073/pnas.0801389105;
RA   Hongoh Y., Sharma V.K., Prakash T., Noda S., Taylor T.D., Kudo T.,
RA   Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT   "Complete genome of the uncultured termite group 1 bacteria in a single
RT   host protist cell.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:5555-5560(2008).
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; AP009510; BAG14094.1; -; Genomic_DNA.
DR   RefSeq; WP_015423618.1; NC_020419.1.
DR   RefSeq; YP_001956555.1; NC_020419.1.
DR   AlphaFoldDB; B1H0R2; -.
DR   SMR; B1H0R2; -.
DR   STRING; 471821.TGRD_611; -.
DR   EnsemblBacteria; BAG14094; BAG14094; TGRD_611.
DR   KEGG; rsd:TGRD_611; -.
DR   PATRIC; fig|471821.5.peg.1019; -.
DR   HOGENOM; CLU_007831_2_2_0; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000001691; 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; 2.
DR   PANTHER; PTHR11806:SF0; PTHR11806:SF0; 2.
DR   Pfam; PF01134; GIDA; 1.
DR   Pfam; PF13932; GIDA_C; 2.
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; tRNA processing.
FT   CHAIN           1..597
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345357"
FT   BINDING         11..16
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         275..289
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   597 AA;  67171 MW;  B73400009450B84D CRC64;
     MERKYNVAVV GAGHAGCEAS LACARMGLKT LIITLNADSM ARMPCNPAVG GIAKGQMVRE
     IDAMGGEIGR ITDRAVLQFK MLNSSRGPAV WSPRAQCDKE LYSVLMSKSV QNQQNLEILQ
     SEATSLTVKN GKVCGVKILT GETIEADAVV ITTGTFLKGT IHLGKMHFNG GRFNEVSALY
     LSKSLIEDCG LKLGRFKTTT TPRINSRSID YSKMTEQFGD EKPVPFSYST KVEEWRKNLK
     QLSCWLTYTN PITHKIVSDN LGLSSIYIGE VNSKSPRYCP SIEEKIERYP EKTSHHVFVE
     PEGYNTNEVY LNGLYTGLPF NLQQQMINSI VGLENAKVIR YGYAIEYDYS SPLQIKKTLE
     TKTVKNLFLG GQINGTTGYE EAAAQGFVAG VNAGLKVLGK TPFILERNES YIGILVDDIT
     TKGMDEPYRM FTSRAEYRLS IRNDNADLRL MDAGHSIGLI SDKAYKKFEL YRKAFTDICE
     NNAENLPDDE DLSPWSIEKA KEEVYIHKKY EGYIEIQNKM INKMKKSKDR KIPEDFDYNK
     LKSLSAETKQ RLFEVRPQTI GQASRICAIK PSDIAILTVY LEKQKKERKQ KKHNKIK