ID   MNMG_SHEB9              Reviewed;         629 AA.
AC   A9KX17;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=Sbal195_4518;
OS   Shewanella baltica (strain OS195).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=399599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS195;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Brettar I.,
RA   Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS195.";
RL   Submitted (NOV-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; CP000891; ABX51675.1; -; Genomic_DNA.
DR   RefSeq; WP_006084766.1; NC_009997.1.
DR   AlphaFoldDB; A9KX17; -.
DR   SMR; A9KX17; -.
DR   EnsemblBacteria; ABX51675; ABX51675; Sbal195_4518.
DR   GeneID; 11774471; -.
DR   KEGG; sbn:Sbal195_4518; -.
DR   HOGENOM; CLU_007831_2_2_6; -.
DR   OMA; FRPGYAI; -.
DR   Proteomes; UP000000770; 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_1000076330"
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;  69286 MW;  15D9CD3915FCB5D7 CRC64;
     MHFHERFDVI VVGGGHAGTE AALAAARMGS KTLLLTHNID TLGQMSCNPA IGGIGKGHLV
     KEIDALGGAM AIATDYAGIQ FRTLNSSKGP AVRATRAQAD RALYRQKIQN ILQNQPNLRI
     FQQAVDDLIV ENHQVVGVVT QMGLAFESPA VVLTTGTFLS GKIHIGLENY SGGRAGDPPA
     IALANRLREL PIRVGRLKTG TPPRIDANTI DFSQMAEQKG DSPLPVMSFM GDVSHHPKQI
     SCWITHTNEK THEIIRGGLD RSPMYSGVIE GIGPRYCPSI EDKIHRFADK SSHQIFIEPE
     GLNTSEIYPN GISTSLPFDV QLNLVRSIKG MENAEIMRPG YAIEYDYFDP RDLKNSLETK
     AINGLFFAGQ INGTTGYEEA GAQGLLAGMN ASLQVQGKEA WCPRRDEAYL GVLVDDLSTL
     GTKEPYRMFT SRAEYRLLLR EDNADIRLTA KGRELGLVDD ARWAAFSEKL ESIELELQRL
     RGQWVHPNSP LIHALNPHLN TPISREASFE ELLRRPEMDY SKLMQIEGFG PGLEDPQAAE
     QVQIQVKYSG YIQRQQEEIN KAVRNENTGL PLTLDYKEVP GLSNEVIAKL NNHKPETIGQ
     ASRISGITPA AISILLVHLK KRGLLRKSA