ID   MNMG_RHIEC              Reviewed;         632 AA.
AC   Q2K2S1;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=RHE_CH04122;
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251;
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(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; CP000133; ABC92865.1; -; Genomic_DNA.
DR   RefSeq; WP_011427302.1; NC_007761.1.
DR   AlphaFoldDB; Q2K2S1; -.
DR   SMR; Q2K2S1; -.
DR   STRING; 347834.RHE_CH04122; -.
DR   EnsemblBacteria; ABC92865; ABC92865; RHE_CH04122.
DR   KEGG; ret:RHE_CH04122; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_5; -.
DR   OMA; FRPGYAI; -.
DR   Proteomes; UP000001936; 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..632
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345321"
FT   BINDING         12..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         271..285
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   632 AA;  68329 MW;  4C4414E24E887C5A CRC64;
     MTNSGYNVIV IGGGHAGTEA ASAAARLGAK TALVTHRRDT IGVMSCNPAI GGLGKGHLVR
     EIDAMDGLMG RVADVAGIQF RMLNRKKGAA VRGPRTQADR KLYRLAMLAA IEATPGLDII
     EGDAFDLDVL DGRVAGVIMK DGRRLQAPAV VLTTGTFLRG LIHIGSEKTP AGRVGEAPSI
     GLSATLARLG LRLGRLKTGT PARLDGKTID WQSVGRQGAD EELVPFSFMT DSITTRQVEC
     GVTRTTEATH RIIVDNIKHS AMYSGQIEGV GPRYCPSIED KLVKFGERDG HQVFLEPEGL
     DDDTVYPNGI STSLPAEIQA AFIKTIPGLE SARILQPGYA IEYDHVDPRE LTPSLEVKRL
     RGLFLAGQIN GTTGYEEAAA QGLAAGLNAA LLSSDSEPFH FSRTSSYIGV MIDDLTSRGV
     TEPYRMFTSR AEYRLTLRAD NADMRLTPLA MALGCVGAER AERFTAYQAE IDAGRAQLMA
     LTVTPNEARR AGLNINLDGQ RRSAYDFLSY PTYDFAALRK VWPEELGRLR PKVAEALEIE
     AGYSVYLDRQ AAAIADQQRD EERRIPADFN YDALSGLSNE LKAKLSAARP FNVAQAAIVE
     GMTPAAVALL LVHLRRQQGF ERQSADTRSE SL