ID   MNMG_MYCCT              Reviewed;         629 AA.
AC   Q2SR15;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=MCAP_0856;
OS   Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS   / NCTC 10154).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=340047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA   Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA   Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000123; ABC01073.1; -; Genomic_DNA.
DR   RefSeq; WP_011387682.1; NC_007633.1.
DR   AlphaFoldDB; Q2SR15; -.
DR   SMR; Q2SR15; -.
DR   EnsemblBacteria; ABC01073; ABC01073; MCAP_0856.
DR   GeneID; 23778190; -.
DR   KEGG; mcp:MCAP_0856; -.
DR   HOGENOM; CLU_007831_2_2_14; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   PhylomeDB; Q2SR15; -.
DR   Proteomes; UP000001928; 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..629
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_1000016623"
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;  70825 MW;  A7DFFBE05E82613C CRC64;
     MKSNYDVIVV GGGHAGVEAA LASARLNKKT ALINLYEDKI ATMPCNPSVG GPAKGIVVRE
     IDALGGEMAK AADATALQTK LLNSSRGPGV WALRVQSDKE EYSKYMRNVI KKQKNLDLIT
     KACTGLVYDD NKSVTGIYLD DEIILNAKAV IITTGTYLKS EILKGIDRYE SGPNNEKTTK
     GISKSLIDLG IKLMRFKTGT PARVYRDSVD LSRAIIEPGT DMKLAFSFST NTYTPIEKQQ
     PCYLIHSTLE TKKIIEDNLE KSAMYSGTVE SIGPRYCPSF EDKVVRFKEK DTHQIFIEPE
     TLNGDTWYVQ GFSTSMPIEV QELMLKSLPG FENVRVKHWA YAIEYDCIDP MQLSPSLELK
     DVRNLFTAGQ INGTSGYEEA AGQGLIAGIN ASRKIDGLDP IILRRDEAYI GVMIDDLINK
     GVWEPYRLLT SRAEHRLLLR NDNAETRLKQ YGREIGLISD TEWEQYLIYV KEIEQAIKEL
     KEIRFTPKSQ LAINLKNKKQ ADLSHGYSGY EIIKIPTVDI NELIEFIPSL QKLKTNQLQS
     IVIEIRFEGY VKKERQLVDK LVKLERKKIP LDINYSKVDN LATEAKDKLE KIRPLNIGQA
     SRITGVNPAD IQMLLFYLKK QYPLESIDD