ID   MNMG_DESAP              Reviewed;         657 AA.
AC   B1I6S1;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=Daud_2232;
OS   Desulforudis audaxviator (strain MP104C).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC   Candidatus Desulforudis.
OX   NCBI_TaxID=477974;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP104C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F., Land M.L.,
RA   Hauser L., Kyrpides N., Ivanova N.N., Richardson P.;
RT   "Complete sequence of chromosome of Desulforudis audaxviator MP104C.";
RL   Submitted (OCT-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; CP000860; ACA60719.1; -; Genomic_DNA.
DR   RefSeq; WP_012303293.1; NC_010424.1.
DR   AlphaFoldDB; B1I6S1; -.
DR   SMR; B1I6S1; -.
DR   STRING; 477974.Daud_2232; -.
DR   EnsemblBacteria; ACA60719; ACA60719; Daud_2232.
DR   KEGG; dau:Daud_2232; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_9; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000008544; 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..657
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345263"
FT   REGION          632..657
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         14..19
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   657 AA;  71825 MW;  86F374192513D668 CRC64;
     MEYTAGKYDV IVVGGGHAGC EAALASARLG CRTLLLTLSI DFVALMPCNP AIGGPGKSHL
     VREIDALGGE MGRNTDRAAI QVRMLNTGKG PAVRALRAQT DKRLYQEGMR RTVEGQPLLD
     LKQAMVEKII VDGGSARGVV TRTGARFLAP AVIVTTGTYL RSRVLVGETS FESGPNGQFP
     AVGLAANLRE NGFELGRFKT GTPPRIDRRT LDFSRMTPQH GDEDCPGFSF AAGNRGKEQI
     QVPCWLTYTT ARTHEIIREN LDRSPLYTGI IQGTGPRYCP SIEDKVVRFA DRERHQVFVE
     PEGLHTNEMY VQGMSTSLPE DVQLLLLRSL PGLEKVEIVR YGYAIEYDYV VPTQLAPTLE
     TKAVSGLFLA GQINGTSGYE EAAAQGIVAG INAAQSVKNG EPLVVSRAQA YIGVLIDDLV
     TKGTREPYRI FTSRAEYRLA LRQDNADLRL TERAHRIGLV SGAHYERFAQ KKDRVRAELE
     RLDRTVVPDP LGRVSRAEVQ DWLAARGSAP LSRPCRLSEL LRRPEIRYAD LVGLGVADPD
     VAPDVAAEVE NQIKYAGYIQ KQAAQVARFE KLEARRIPAD LDYSEVRGLS NEAAQKLAEI
     RPVSVGQAGR ISGVSPADIA VLLVYLEKRR RREEESDGSR IGHLPSERSG ELGSGTG