ID   MNMG_RICM5              Reviewed;         622 AA.
AC   A8F0G3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=RMA_0091;
OS   Rickettsia massiliae (strain Mtu5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=416276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mtu5;
RX   PubMed=17916642; DOI=10.1101/gr.6742107;
RA   Blanc G., Ogata H., Robert C., Audic S., Claverie J.-M., Raoult D.;
RT   "Lateral gene transfer between obligate intracellular bacteria: evidence
RT   from the Rickettsia massiliae genome.";
RL   Genome Res. 17:1657-1664(2007).
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; CP000683; ABV84399.1; -; Genomic_DNA.
DR   RefSeq; WP_012152380.1; NC_009900.1.
DR   AlphaFoldDB; A8F0G3; -.
DR   SMR; A8F0G3; -.
DR   EnsemblBacteria; ABV84399; ABV84399; RMA_0091.
DR   KEGG; rms:RMA_0091; -.
DR   HOGENOM; CLU_007831_2_2_5; -.
DR   OMA; FRPGYAI; -.
DR   Proteomes; UP000001311; 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..622
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_1000057845"
FT   BINDING         10..15
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         122
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         177
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         269..283
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         366
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   622 AA;  68815 MW;  B4E60F02B013F6ED CRC64;
     MLKYDVIVIG GGHAGVEAAA ASARLGVPTL LITLKPENLG EMSCNPAIGG IAKGTLVKEI
     DALDGLMGYV IDQAGIHYKM LNETRGPAVW GPRAQADRKL YKKAMYQILT NYPNLDILYG
     KVEDIEIKSS KIEAVILNNG SKILCQKIIL TTGTFLSGLI HIGQKKIPAG RVDEEPSYGL
     SNTLKQIGFK LARLKTGTPP RIDGRTIDYS KTILQPGDKI PRPFSELTNI VNVSQINCFI
     TKTTSETHDI IRENLDKSAM YSGQIEGIGP RYCPSIEDKI VRFSTKSEHR IFLEPEGLDD
     YTIYPNGIST SLPEDVQHKL IKTIPGLENV KVLRPGYAIE YDYVDPREIS VTLETKKIAG
     LYFAGQINGT TGYEEAAGQG IIAGINAALA VKDQAPFMLT RANSYIGVMI DDLTTFGTIE
     PYRMFTSRSE YRLSLRADNS DLRLTELGMN IGVVSEKRKK IFTKKCEDIE KIKSLLNTLS
     LTTSKLAKMG IQVAQDGTYK TVLDLFKIPN FNVEQAIKIF PMLKETQNNN ILQLLYIEAK
     YASYLTRQHA DINLFQSEEA QLIPKNIDYF KIPSISLEIQ EKLSSHKPTT IGVARRIPGI
     TPAAITAIII YLKTKYSDGS ST