ID   MNMG_MYCMS              Reviewed;         629 AA.
AC   Q6MRU5;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=mnmG1 {ECO:0000255|HAMAP-Rule:MF_00129};
GN   Synonyms=gidA1 {ECO:0000255|HAMAP-Rule:MF_00129};
GN   OrderedLocusNames=MSC_1017;
GN   and
GN   Name=mnmG2 {ECO:0000255|HAMAP-Rule:MF_00129};
GN   Synonyms=gidA2 {ECO:0000255|HAMAP-Rule:MF_00129};
GN   OrderedLocusNames=MSC_1042;
OS   Mycoplasma mycoides subsp. mycoides SC (strain PG1).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG1;
RX   PubMed=14762060; DOI=10.1101/gr.1673304;
RA   Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J.,
RA   Johansson K.-E., Pettersson B., Uhlen M.;
RT   "The genome sequence of Mycoplasma mycoides subsp. mycoides SC type strain
RT   PG1T, the causative agent of contagious bovine pleuropneumonia (CBPP).";
RL   Genome Res. 14:221-227(2004).
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; BX293980; CAE77646.1; -; Genomic_DNA.
DR   EMBL; BX293980; CAE77623.1; -; Genomic_DNA.
DR   RefSeq; NP_975981.1; NC_005364.2.
DR   RefSeq; NP_976004.1; NC_005364.2.
DR   AlphaFoldDB; Q6MRU5; -.
DR   SMR; Q6MRU5; -.
DR   STRING; 272632.MSC_1017; -.
DR   EnsemblBacteria; CAE77623; CAE77623; MSC_1017.
DR   EnsemblBacteria; CAE77646; CAE77646; MSC_1042.
DR   KEGG; mmy:MSC_1017; -.
DR   KEGG; mmy:MSC_1042; -.
DR   PATRIC; fig|272632.4.peg.1104; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_14; -.
DR   OMA; FRPGYAI; -.
DR   Proteomes; UP000001016; 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; Reference proteome; tRNA processing.
FT   CHAIN           1..629
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000117135"
FT   BINDING         11..16
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         273..287
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   629 AA;  70741 MW;  EF1F2B23C88FC8CF CRC64;
     MKSNYDVIVV GGGHAGVEAA LASARLNKKT ALINLYEDKI ATMPCNPSVG GPAKGIVVRE
     IDALGGEMAK AADATALQTK LLNSSRGPGV WALRVQSDKE EYSKYMRNVI KNQKNLDLIT
     RACTGLVYDE NKTVTGIYLD DQTILNAKAV IITTGTYLKS EILKGVDRYE SGPNNEKTTK
     GISQSLIDLG IKLMRFKTGT PARVYRDSVD LSNAVLEPGT DMKLAFSFST STYTPIEKQQ
     PCYLIHSTLE TKKIIEDNLE KSAMYSGTVK SIGPRYCPSF EDKAVRFREK DTHQIFIEPE
     TLNGDTWYVQ GFSTSMPIEV QEMMLKSLPG FENVRVKHWA YAIEYDCIDP MQLSPSLELK
     DVKNLFTAGQ INGTSGYEEA AGQGLIAGIN ASRKIDGLDP IILRRDEAYI GVMIDDLINK
     GVWEPYRLLT SRAEHRLLLR NDNAETRLKQ YGKEIGLISD QEWNQYLIYV KEIEQAIKEL
     KEIRFTPKSQ LAINLKNKNQ ADLSHGYSGY EIIKIPTVDI NELIEFIPSL QKLKTNQLQS
     IVIEIRFEGY VKKERQLVDK LVKLERKKIP LDINYSKVDN LATEAKDKLE KIRPLNIGQA
     SRITGVNPAD IQMLLFYLKK QYPLENIDN