ID   MNMG_ROSCS              Reviewed;         676 AA.
AC   A7NN26;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=Rcas_2896;
OS   Roseiflexus castenholzii (strain DSM 13941 / HLO8).
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Roseiflexineae;
OC   Roseiflexaceae; Roseiflexus.
OX   NCBI_TaxID=383372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13941 / HLO8;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Bryant D.A., Hanada S., Tsukatani Y., Richardson P.;
RT   "Complete sequence of Roseiflexus castenholzii DSM 13941.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000804; ABU58958.1; -; Genomic_DNA.
DR   RefSeq; WP_012121382.1; NC_009767.1.
DR   AlphaFoldDB; A7NN26; -.
DR   SMR; A7NN26; -.
DR   STRING; 383372.Rcas_2896; -.
DR   EnsemblBacteria; ABU58958; ABU58958; Rcas_2896.
DR   KEGG; rca:Rcas_2896; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_0; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000000263; 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   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..676
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345326"
FT   BINDING         15..20
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         316..330
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   676 AA;  74761 MW;  6EF8967ABE2F3785 CRC64;
     MDSIHPFIYD LIVVGAGHAG CEAAHAAARM GCRTLLLTID LDKLAHMSCN PSIGGPAKGH
     LVREIDALGG LMGRVTDRTF IQIRLLNESK GPAVQAPRAQ ADKRLYAKVM KETLETTPNL
     DLRQAMIERI LLPQPPGRNG SAAPADDPAG VQPGHYAVIT HTRRVYQSRA LVLTTGTFLR
     GRAITGEAIW GAGRAGEAPA TALGEDLAAL GFPLVRLKTG TPPRIDARTI DFSQTSVQQG
     SPTPLFFGHY YRVLGEIPPE PAFTGAPACA YPEPLRAAWR PQLPCYLVHT TPEFHEIVRR
     NLDRAPLFSG IIEGVGPRYC PSIEDKIVRF ADKERHGLFL EPEGWSTHEV YVQGCNTSLP
     EDVQWAMLRS IPALRRVELM RAGYAIEYDA LATGEIAADM SSRRIPGLFF AGQINGTTGY
     EEAAAQGLMA GINAARFIQG KPPIILRRDE AYIGVLIDDL ITKEIREPYR MFTSRAEHRL
     LLRTDNADLR LTRLAGELGL VDRERVEAVE RKREESERLL RVLRGQRLFP SAATNARLSD
     VGIAPLSSEM SAEDVLRRPE VRYEQLRQAL DLPACDADIA EQVEIEAKYG GYLQKQQREV
     ERLRRMEARR IPPDFDFTAL RGLRNEARQT LQRFRPATVG QAARLAGINP ADVAILIVAL
     ERRGRRDMAL DVRSGA