ID   MNMG_RALPJ              Reviewed;         649 AA.
AC   B2UGW0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=Rpic_3523;
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12J;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome 1 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-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; CP001068; ACD28643.1; -; Genomic_DNA.
DR   RefSeq; WP_012436731.1; NC_010682.1.
DR   AlphaFoldDB; B2UGW0; -.
DR   SMR; B2UGW0; -.
DR   STRING; 402626.Rpic_3523; -.
DR   EnsemblBacteria; ACD28643; ACD28643; Rpic_3523.
DR   KEGG; rpi:Rpic_3523; -.
DR   PATRIC; fig|402626.5.peg.4660; -.
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..649
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_1000095658"
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   649 AA;  70809 MW;  EA0D620CD9444A11 CRC64;
     MLYPIEFDVI VVGGGHAGTE AALAAARMGC QTLLLTHNIE TLGQMSCNPS IGGIGKGHLV
     KEVDALGGAM AIATDEGGIQ FRILNSSKGP AVRATRAQAD RVLYKAAIRH RLENQPNLML
     FQQAVEDLVV EGDRVIGAVT QVGVQFRARA VVLTAGTFLD GKIHVGLNNY TGGRAGDPAA
     VSLSARLKEL KLPQGRLKTG TPPRIDGRSI DFSVLEEQPG DLDPVPVFSF MGRADMHPRQ
     VPCWVTHTNE RTHDIIRAGL DRSPMYTGVI EGVGPRYCPS IEDKIHRFAS KDSHQIFLEP
     EGLATNEFYP NGVSTSLPFD VQLDLIHSMR GLENAHILRP GYAIEYDYFD PRGLKASLES
     KAISGLFFAG QINGTTGYEE AAAQGLLAGI NAGLQVQGKD AWTPRRDQAY LGVLVDDLIT
     RGVTEPYRMF TSRAEFRLSL REDNADMRLT EVGRTLGVVD DARWDAFNRK RDAVSRETER
     LKSTWVNPAT LPLEDAEPVL GKGIEREYAL ADLLRRPNVT YETLVGMQGG KYALESPLAE
     DPLLAEQIRE QVEIGIKYHG YIARQADEVE RLGANENTRL PADFDYSQVR GLSIEVQQKL
     AKHKPETIGQ ASRISGITPA AVSLLLVHLK KGVLRGQVGP RASSEGEAA