ID   MNMG_POLNS              Reviewed;         640 AA.
AC   B1XSC4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=Pnec_0012;
OS   Polynucleobacter necessarius subsp. necessarius (strain STIR1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=452638;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STIR1;
RX   PubMed=24167248; DOI=10.1073/pnas.1316687110;
RA   Boscaro V., Felletti M., Vannini C., Ackerman M.S., Chain P.S.,
RA   Malfatti S., Vergez L.M., Shin M., Doak T.G., Lynch M., Petroni G.;
RT   "Polynucleobacter necessarius, a model for genome reduction in both free-
RT   living and symbiotic bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:18590-18595(2013).
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; CP001010; ACB43342.1; -; Genomic_DNA.
DR   RefSeq; WP_012357111.1; NC_010531.1.
DR   AlphaFoldDB; B1XSC4; -.
DR   SMR; B1XSC4; -.
DR   STRING; 452638.Pnec_0012; -.
DR   EnsemblBacteria; ACB43342; ACB43342; Pnec_0012.
DR   KEGG; pne:Pnec_0012; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_4; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
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..640
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_1000095656"
FT   BINDING         13..18
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         274..288
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   640 AA;  70031 MW;  A083FF267009DCD0 CRC64;
     MRYSKNFDVI VVGGGHAGTE AALASARMGC DTLLITHSIE NLGAMSCNPS IGGIGKGHLV
     KEIDAMGGAM AAATDEAGIQ FRILNSSKGP AVRATRAQGD RVLYKAAIRR RLENQPNLSL
     FQAAVDDLPV KGDEVQGVVT QMGLEFMAKK VVLTAGTFLD GKIHVGLNNY AGGRAGDPAA
     VSLSARLKEL KLPQGRLKTG TPPRIDGLTI DFSVMLEQPG DLDPVPVFSY LGRPEQHPKQ
     VPCWISHTNE KTHDIIRGGL DRSPMYTGVI KGVGPRYCPS IEDKIHRFAS RNSHQIFLEP
     EGLTTNEFYP NGISTSLPFD VQWDLVRSIR GMESAVIVRP GYAIEYDFFD PRQLRHSLET
     KVIGGLYFAG QINGTTGYEE AAAQGMLAGI NAGLAAKGKE PWLPKRSESY IGVLVDDLIA
     RGVQEPYRMF TSRAEYRLSL REDNADMRLT AIGRDLGLVD DYRWGVFCRK QEAVSRETSR
     LQNIWVGPKS EAAPFVSQLL DQDLSHESSL AELLRRPGVT YESIIALGDG MWAPETLDED
     LGLAAQISDQ VEISVKYQGY IERQATEIAR QEHNETLLLP ESLDYSQVIG LSKEVQQKLN
     LHKPETLGQA GRISGVTPAA LSLLLVHLKK DLGHTQEAHE