ID   MNMG_SULMW              Reviewed;         611 AA.
AC   A8Z5Q4;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-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=SMGWSS_024;
OS   Sulcia muelleri (strain GWSS).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Candidatus Sulcia.
OX   NCBI_TaxID=444179;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GWSS;
RX   PubMed=18048332; DOI=10.1073/pnas.0708855104;
RA   McCutcheon J.P., Moran N.A.;
RT   "Parallel genomic evolution and metabolic interdependence in an ancient
RT   symbiosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:19392-19397(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; CP000770; ABS30454.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8Z5Q4; -.
DR   SMR; A8Z5Q4; -.
DR   STRING; 444179.SMGWSS_024; -.
DR   EnsemblBacteria; ABS30454; ABS30454; SMGWSS_024.
DR   KEGG; smg:SMGWSS_024; -.
DR   HOGENOM; CLU_007831_2_2_10; -.
DR   OMA; FRPGYAI; -.
DR   Proteomes; UP000000781; 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..611
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345341"
FT   BINDING         12..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         271..285
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   611 AA;  69486 MW;  69A857D1A34EB9C9 CRC64;
     MFVKQYDVIV VGGGHSGSEA ALAASNLGSN TLLITTNLYN IGQMSCNPAM GGIAKGQMIK
     EIDALGGYSG IITDKSMIQF RMLNKSKGPA MWSPRAQCDR LKFSKEWRLT LEKKKNLSFF
     QSTVVDLIIK NYKVIGVKTI LGIYIKSKSV ILTNGTFLNG IIHIGDKKNS GGRISENSVK
     GLTEKLKKIG FFSGRMKTGT SPRLDGRSLD FSKMIEQLGD FPIEPFSYLS NLNILKQKKC
     YITHTNLETH NLLSKEFNRS PIFNGKIKCV GPRYCPSIEE KVYRFSNKEN HQIFVEPEGV
     NTIEVYINGF STSMPEEVQY KALLTIPGFE HAKMVRPGYA IEYDYFPPTQ LKNNLETKLI
     ENLFFAGQIN GTTGYEEAAA QGLIAGINAN LKINEKDPFI LKRNEAYIGV LIDDLIYKGT
     EEPYRMFTSR AEYRILLRQD NADERLTHMG INLGLVSYDR IKKLKNKNKN KKQCFLFFKI
     NKANNLILKE NIKICDLLSR PEISIYDIIK LSLIKNFIKK NNIDKKILEQ ISLYIKYKGY
     LLKEEENVKK MYRLETIRIP NDFDYNQVKS ISIEAREKLL NYKPNSIGEA SRISGVSPSD
     IRILILFLIK K