ID   MNMG_MANSM              Reviewed;         629 AA.
AC   Q65PZ9;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=MS2354;
OS   Mannheimia succiniciproducens (strain MBEL55E).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Basfia.
OX   NCBI_TaxID=221988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBEL55E;
RX   PubMed=15378067; DOI=10.1038/nbt1010;
RA   Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA   Jeong H., Hur C.G., Kim J.J.;
RT   "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT   succiniciproducens.";
RL   Nat. Biotechnol. 22:1275-1281(2004).
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; AE016827; AAU38961.1; -; Genomic_DNA.
DR   RefSeq; WP_011201499.1; NC_006300.1.
DR   AlphaFoldDB; Q65PZ9; -.
DR   SMR; Q65PZ9; -.
DR   STRING; 221988.MS2354; -.
DR   EnsemblBacteria; AAU38961; AAU38961; MS2354.
DR   KEGG; msu:MS2354; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_6; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000000607; 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; tRNA processing.
FT   CHAIN           1..629
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000117128"
FT   BINDING         13..18
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   629 AA;  70169 MW;  49A93449F7AE13E8 CRC64;
     MFYSENYDVI VIGGGHAGTE AALAPARMGL KTLLLTHNID TLGQMSCNPA IGGIGKGHLV
     KEIDAMGGLM ATAADQAGIQ FRTLNSSKGP AVRATRAQAD RVLYRQAVKV ALENQPNLDI
     FQQEATDILI EQDRVTGVAT RMGLKFKTKS VILTAGTFLG GKIHIGLDNY TGGRAGDPAS
     IALADRLRDL NLRVARLKTG TPPRLDARTI NFDILAKQHG DAQLPVFSFM GSVDQHPRQI
     PCFITHTNEQ THEVIRNNLD RSPMYTGVIE GIGPRYCPSI EDKVMRFADR NSHQIYLEPE
     GLTSQEIYPN GISTSLPFDV QMKIVNSMVG LEKTRIVKPG YAIEYDFFDP RDLKPTLETK
     AIKGLFFAGQ INGTTGYEEA ASQGLLAGIN AGLFVQEKES WFPRRDQAYM GVLVDDLCTL
     GTKEPYRVFT SRAEYRLLLR EDNADSRLTP IAHELGLIDE NRWARFNQKM ENIERERQRL
     RNIWIHPRSE HLDVINEVLS SPLVREASGE DLLRRPEINY QILTALDLFK PAMDDKEAVE
     QVEIAVKYQG YIEHQQEEIE KQKRHENTAI PDNFDYTLVA GLSNEVRAKL EQHRPVSIGQ
     ASRISGVTPA AISILLVNLK KQGMLKRGE