ID   MNMG_UREP2              Reviewed;         614 AA.
AC   B1AI24;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=UPA3_0038;
OS   Ureaplasma parvum serovar 3 (strain ATCC 27815 / 27 / NCTC 11736).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=505682;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27815 / 27 / NCTC 11736;
RA   Methe B.A., Glass J., Waites K., Shrivastava S.;
RT   "Genome sequence of Ureaplasma parvum serovar 3.";
RL   Submitted (FEB-2008) 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; CP000942; ACA32872.1; -; Genomic_DNA.
DR   RefSeq; WP_010891662.1; NC_010503.1.
DR   AlphaFoldDB; B1AI24; -.
DR   SMR; B1AI24; -.
DR   EnsemblBacteria; ACA32872; ACA32872; UPA3_0038.
DR   GeneID; 29672170; -.
DR   KEGG; upa:UPA3_0038; -.
DR   HOGENOM; CLU_007831_2_2_14; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000002162; 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..614
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_1000076338"
FT   BINDING         10..15
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         271..285
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   614 AA;  69193 MW;  5DFC22A8B3B70ACF CRC64;
     MKKYDVIVIG AGHAGLEAAF ATSNLNLQTA LITLDEKGIG MMPCNPSIGG PAKGIVTREI
     DALGGIQGKA ADATTMQMKI LNSSKGPGVW AIRAQIDKIA YQRWFKQQIK QQKNLDLIIA
     EVSDLLVENN IVKGVVLSDQ KIIQADYVII TTGTYLKSIT HRGSVCVDEG ADGTKNAKFL
     SDALVKLGFE LIRLKTGTPA RIKKDSIDFT NMILEPGTNQ KIAFSHYHPV YKPYDEQLPC
     HIIYTNEQTH QIIRENLNKS AMYGGMISGI GPRYCPSIED KIVKFSEKPR HQIFVEPESY
     ELDSMYLGGF STSMPIDVQE KMIRSLPGLE NCEILKYAYA IEYDAIDPTQ LYPSLESKLV
     NNLFFAGQIN GTSGYEEAAA QGLMAAINVN QKYQNKEPVI LGRDQAYIGV MIDDIVTKGV
     VEPYRLLTSR AEHRLALRND NADDRLMKIG FEIGLLKPEV YDQYLNNLKQ IKEILNWLKT
     TTVGQIDDLK FTTLKTNSYL IDYLKRPEIK LNDLLIYCPI KIEDEQIINK VQIQVKFEGY
     IKNQEENLKQ LKRLNNIKLH AIVDYKEVPN ISLETIDKLN KIKPLDLEQA SRISGVNLTD
     IAMIKYYLER IKND