MNMG_STRPM
ID MNMG_STRPM Reviewed; 632 AA.
AC Q48QN0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=M28_Spy1870;
OS Streptococcus pyogenes serotype M28 (strain MGAS6180).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=319701;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS6180;
RX PubMed=16088825; DOI=10.1086/430618;
RA Green N.M., Zhang S., Porcella S.F., Nagiec M.J., Barbian K.D., Beres S.B.,
RA Lefebvre R.B., Musser J.M.;
RT "Genome sequence of a serotype M28 strain of group A Streptococcus:
RT potential new insights into puerperal sepsis and bacterial disease
RT specificity.";
RL J. Infect. Dis. 192:760-770(2005).
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; CP000056; AAX72980.1; -; Genomic_DNA.
DR RefSeq; WP_011285326.1; NC_007296.2.
DR AlphaFoldDB; Q48QN0; -.
DR SMR; Q48QN0; -.
DR EnsemblBacteria; AAX72980; AAX72980; M28_Spy1870.
DR KEGG; spb:M28_Spy1870; -.
DR HOGENOM; CLU_007831_2_2_9; -.
DR OMA; FRPGYAI; -.
DR Proteomes; UP000009292; 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..632
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_1000016694"
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; 70141 MW; A96FA1C53DB47B55 CRC64;
MTHEFTESYD VIVIGAGHAG VEASLATSRM GCKTLLATIN LDMLAFMPCN PSIGGSAKGI
VVREIDALGG EMGKNIDKTY IQMKMLNTGK GPAVRALRAQ ADKSLYAREM KHTVEKQANL
TLRQTMIDDI LVEDGRVVGV LTATGQKFAA KAVVVTTGTA LRGEIILGEL KYSSGPNNSL
ASVTLADNLK KLGLEIGRFK TGTPPRVKAS SINYDQTEIQ PGDDKPNHFS FMSKDAEYLK
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