MNMG_STRPQ
ID MNMG_STRPQ Reviewed; 632 AA.
AC P0DB35; Q8K5H7;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 48.
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}; OrderedLocusNames=SPs1834;
OS Streptococcus pyogenes serotype M3 (strain SSI-1).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=193567;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSI-1;
RX PubMed=12799345; DOI=10.1101/gr.1096703;
RA Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y.,
RA Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T., Hayashi H.,
RA Hattori M., Hamada S.;
RT "Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-
RT scale genomic rearrangement in invasive strains and new insights into phage
RT evolution.";
RL Genome Res. 13:1042-1055(2003).
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; BA000034; BAC64929.1; -; Genomic_DNA.
DR RefSeq; WP_011055105.1; NC_004606.1.
DR AlphaFoldDB; P0DB35; -.
DR SMR; P0DB35; -.
DR KEGG; sps:SPs1834; -.
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_0000411355"
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; 70129 MW; 00C9A4B84CBA82CE 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 KSELILKRSD AYIGVMIDDL
VTKGTLEPYR LLTSRAEYRL ILRHDNADMR LTEIGRDIGL VDDERWKAFE IKKNQFDNEL
KRLNSIKLKP VKATNDRVQE LGFKPLTDAM TAKEFMRRPE IDYAIAVSFV GPAAEDLDAK
IIELLETEIK YEGYIRKALD QVAKMKRMEE KRIPANIDWD AIDSIATEAR QKFKKINPET
IGQASRISGV NPADISILMI YLEGNGKAHR KY