ID   MNMG_STRPG              Reviewed;         632 AA.
AC   A2RH03;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=SpyM51810;
OS   Streptococcus pyogenes serotype M5 (strain Manfredo).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=160491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Manfredo;
RX   PubMed=17012393; DOI=10.1128/jb.01227-06;
RA   Holden M.T.G., Scott A., Cherevach I., Chillingworth T., Churcher C.,
RA   Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Moule S., Mungall K., Quail M.A., Price C., Rabbinowitsch E., Sharp S.,
RA   Skelton J., Whitehead S., Barrell B.G., Kehoe M., Parkhill J.;
RT   "Complete genome of acute rheumatic fever-associated serotype M5
RT   Streptococcus pyogenes strain Manfredo.";
RL   J. Bacteriol. 189:1473-1477(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; AM295007; CAM31135.1; -; Genomic_DNA.
DR   RefSeq; WP_002982082.1; NC_009332.1.
DR   AlphaFoldDB; A2RH03; -.
DR   SMR; A2RH03; -.
DR   KEGG; spf:SpyM51810; -.
DR   HOGENOM; CLU_007831_2_2_9; -.
DR   OMA; FRPGYAI; -.
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..632
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_1000016693"
FT   BINDING         15..20
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         127
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         182
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         276..290
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         373
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   632 AA;  70127 MW;  D905AACEA8CF5525 CRC64;
     MTHEFTESYD VIVIGAGHAG VEASLATSRM GCKTLLATIN LDMLAFMPCN PSIGGSAKGI
     VVREIDALGG EMGKNIDKTY IQMKMLNTGK GPAVRALRAQ ADKSLYAREM KHTVEKQANL
     TLRQTMIDDI LVEDGRVVGV LTATGQKFAA KAVVVTTGTA LRGEIILGEL KYSSGPNNSL
     ASVTLADNLK KLGLEIGRFK TGTPPRVKAS SINYDQTEIQ PGDDKPNHFS FMSKDADYLK
     DQIPCWLTYT NQTSHDIINQ NLYRAPMFSG IVKGVGPRYC PSIEDKIVRF ADKERHQLFL
     EPEGRDTEEV YVQGLSTSLP EDVQKDLIHS IKGLEKAEMM RTGYAIEYDI VLPHQLRATL
     ETKLISGLFT AGQTNGTSGY EEAAGQGLIA GINAALKVQG KPELILKRSD AYIGVMIDDL
     VTKGTLEPYR LLTSRAEYRL ILRHDNADMR LTEIGRDIGL VDDERWKAFE IKKNQFDNEL
     KRLNSIKLKP VKATNDRVQE LGFKPLTDAM TAKEFMRRPE IDYATAVSFV GPAAEDLDAK
     IIELLETEIK YEGYIRKALD QVAKMKRMEE KRIPANIDWD AIDSIATEAR QKFKKINPET
     IGQASRISGV NPADISILMI YLEGNGKAHR KY