ID MNMG_STRP8 Reviewed; 632 AA.
AC Q8NZ02;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 29-MAY-2013, entry version 68.
DE RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG;
DE AltName: Full=Glucose-inhibited division protein A;
GN Name=mnmG; Synonyms=gidA; OrderedLocusNames=spyM18_2220;
OS Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=186103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS8232;
RX PubMed=11917108; DOI=10.1073/pnas.062526099;
RA Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F.,
RA Parkins L.D., Beres S.B., Campbell D.S., Smith T.M., Zhang Q.,
RA Kapur V., Daly J.A., Veasy L.G., Musser J.M.;
RT "Genome sequence and comparative microarray analysis of serotype M18
RT group A Streptococcus strains associated with acute rheumatic fever
RT outbreaks.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
CC -!- FUNCTION: NAD-binding protein involved in the addition of a
CC carboxymethylaminomethyl (cmnm) group at the wobble position (U34)
CC of certain tRNAs, forming tRNA-cmnm(5)s(2)U34 (By similarity).
CC -!- COFACTOR: FAD (By similarity).
CC -!- SUBUNIT: Homodimer (By similarity). Heterotetramer of two MnmE and
CC two MnmG subunits (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the MnmG family.
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DR EMBL; AE009949; AAL98654.1; -; Genomic_DNA.
DR RefSeq; NP_608155.1; NC_003485.1.
DR ProteinModelPortal; Q8NZ02; -.
DR STRING; 186103.spyM18_2220; -.
DR EnsemblBacteria; AAL98654; AAL98654; spyM18_2220.
DR GeneID; 995159; -.
DR KEGG; spm:spyM18_2220; -.
DR PATRIC; 19750827; VBIStrPyo4396_1977.
DR eggNOG; COG0445; -.
DR HOGENOM; HOG000201060; -.
DR KO; K03495; -.
DR OMA; AQMSCNP; -.
DR ProtClustDB; PRK05192; -.
DR BioCyc; SPYO186103:GHJG-1894-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:HAMAP.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR HAMAP; MF_00129; MnmG_GidA; 1; -.
DR InterPro; IPR004416; GidA.
DR InterPro; IPR026904; GidA-assoc_3.
DR InterPro; IPR002218; GIDA-rel.
DR InterPro; IPR020595; GIDA-rel_CS.
DR Pfam; PF01134; GIDA; 1.
DR Pfam; PF13932; GIDA_assoc_3; 1.
DR TIGRFAMs; TIGR00136; gidA; 1.
DR PROSITE; PS01280; GIDA_1; 1.
DR PROSITE; PS01281; GIDA_2; 1.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; FAD; Flavoprotein; NAD; tRNA processing.
FT CHAIN 1 632 tRNA uridine 5-carboxymethylaminomethyl
FT modification enzyme MnmG.
FT /FTId=PRO_0000117190.
FT NP_BIND 15 20 FAD (By similarity).
FT NP_BIND 276 290 NAD (Potential).
FT BINDING 127 127 FAD; via amide nitrogen and carbonyl
FT oxygen (By similarity).
FT BINDING 182 182 FAD (By similarity).
FT BINDING 373 373 FAD (By similarity).
SQ SEQUENCE 632 AA; 70157 MW; 3E80038FF60F5522 CRC64;
MTHEFTESYD VIVIGAGHAG VEASLATSRM GCKTLLATIN LDMLAFMPCN PSIGGSAKGI
VVREIDALGG EMSKNIDKTY 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
//
