ID MNMG_STRSV Reviewed; 635 AA.
AC A3CRB1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 101.
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=SSA_2359;
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36;
RX PubMed=17277061; DOI=10.1128/jb.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(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; CP000387; ABN45716.1; -; Genomic_DNA.
DR RefSeq; WP_011837713.1; NC_009009.1.
DR RefSeq; YP_001036266.1; NC_009009.1.
DR AlphaFoldDB; A3CRB1; -.
DR SMR; A3CRB1; -.
DR STRING; 388919.SSA_2359; -.
DR KEGG; ssa:SSA_2359; -.
DR PATRIC; fig|388919.9.peg.2240; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_9; -.
DR OrthoDB; 9815560at2; -.
DR Proteomes; UP000002148; 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; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.150.570; GidA associated domain, C-terminal subdomain; 1.
DR Gene3D; 1.10.10.1800; tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG/GidA; 1.
DR HAMAP; MF_00129; MnmG_GidA; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR049312; GIDA_C_N.
DR InterPro; IPR004416; MnmG.
DR InterPro; IPR002218; MnmG-rel.
DR InterPro; IPR020595; MnmG-rel_CS.
DR InterPro; IPR026904; MnmG_C.
DR InterPro; IPR047001; MnmG_C_subdom.
DR InterPro; IPR044920; MnmG_C_subdom_sf.
DR InterPro; IPR040131; MnmG_N.
DR NCBIfam; TIGR00136; gidA; 1.
DR PANTHER; PTHR11806; GLUCOSE INHIBITED DIVISION PROTEIN A; 1.
DR PANTHER; PTHR11806:SF0; PROTEIN MTO1 HOMOLOG, MITOCHONDRIAL; 1.
DR Pfam; PF01134; GIDA; 1.
DR Pfam; PF13932; GIDA_C; 1.
DR Pfam; PF21680; GIDA_C_1st; 1.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM01228; GIDA_assoc_3; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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..635
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_1000016696"
FT BINDING 15..20
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"
SQ SEQUENCE 635 AA; 70832 MW; 4EA939EAB1968F8E CRC64;
MSHNFTESYD IIVIGAGHAG VEASLAASRM GCKVLLATIN IEMLAFMPCN PSIGGSAKGI
VVREVDALGG EMAKNIDKSY IQMKMLNTGK GPAVRALRAQ ADKELYSKEM RKTVENQENL
TLRQTMINEI LVEDGKVIGV KTATHQEYAA KAVIVTTGTA LRGEIIIGDL KYSSGPNHSL
AAIPLADNLR DLGFEIGRFK TGTPPRVKAS SINYDVTEIQ PGDEKANHFS YTSRDEDYVK
DQVPCWLTYT NAESHEIIQN NLHRAPMFSG IVKGVGPRYC PSIEDKIVRF ADKERHQLFL
EPEGRDTEEV YVQGLSTSLP EDVQKDLVHS IKGLENAEMM RTGYAIEYDM IMPHQLRATL
ETKKISGLFT AGQTNGTSGY EEAAGQGIIA GINAALKIQG KQELILKRSD GYIGVMIDDL
VTKGTVEPYR LLTSRAEYRL ILRHDNADMR LTEMGREIGL VDDERWARFE IKKNQFDNEM
KRLESIKLKP VKETNAKVEA LGFKPLTDAV TAKEFMRRPE VSYQDVVQFI GPAAEELDEK
IIELIETEIK YEGYISKALD QVEKMKRMEE KRIPANIDWD DIDSIATEAR QKFKKINPET
IGQASRISGV NPADISILMV YLEGKSRSIS KNQAK
//
