ID   MNMG_MYCPN              Reviewed;         612 AA.
AC   P75221;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 117.
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}; OrderedLocusNames=MPN_557;
GN   ORFNames=MP285;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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; U00089; AAB95933.1; -; Genomic_DNA.
DR   PIR; S73611; S73611.
DR   RefSeq; NP_110246.1; NC_000912.1.
DR   RefSeq; WP_010874914.1; NC_000912.1.
DR   AlphaFoldDB; P75221; -.
DR   SMR; P75221; -.
DR   IntAct; P75221; 1.
DR   STRING; 272634.MPN_557; -.
DR   EnsemblBacteria; AAB95933; AAB95933; MPN_557.
DR   GeneID; 66608761; -.
DR   KEGG; mpn:MPN_557; -.
DR   PATRIC; fig|272634.6.peg.619; -.
DR   HOGENOM; CLU_007831_2_2_14; -.
DR   OMA; FRPGYAI; -.
DR   BioCyc; MPNE272634:G1GJ3-914-MON; -.
DR   Proteomes; UP000000808; 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..612
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000117137"
FT   BINDING         9..14
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         270..284
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   612 AA;  68053 MW;  35DFF3A14395BC2C CRC64;
     MSFTLTVIGG GHAGLEAAFI ASKLGLKVNL LVLDPNHVGS CPCNPAIGGP AKGIVTREID
     VLGGMQGKAA DATALQYKLL NSSKGPAVQA IRAQIDKIAY QKWFRQQIDQ TPNIELIAGE
     AVDILESNGK VKGVVLADGS ELASDAVIVT TGTYLKAKTY CGSLSKEEGP DRAKRSEYLS
     TNLIKRGFKT LRLKTGTPPR ILRESLDFSQ MAVEANTTPH LAFSFTTKNY LPLEQQVICH
     LIHTNPQIHQ LILANLKQSA VFNGSIKANG PLYCPSIEDK VFRFQDKERH QIFVEPESLS
     LETVYLAGFS TSFPPEVQEH IVRLLPGFKN ARFQKYGYAI EYDAFSSIQL KSTLETKLIQ
     NLYFAGQING TSGYEEAAGQ GLIAGINAAL KLQRKPEFVL QRNEAYLGVM INDLVTKEIS
     DPYRLLTSRA EHRLWLRNDN LQERLIEKSR ALGLVEADVY ANYLEQQQKK KQLIDYLQTT
     TVGQIAALKL NFKNTAQTLF DFTKRAEIKL VDLVQLLPKR FDLDVQSLNQ IDIDIKYAGY
     IKKSEKYFKS LNNLSSVKIP LKLNYHKVPN LASEAIVKLS KIRPTDLSVA SQVAGINFND
     ILAIKHFLDN HE