ID   MNMG_CUPMC              Reviewed;         654 AA.
AC   Q1LHJ8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=Rmet_3506;
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
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; CP000352; ABF10378.1; -; Genomic_DNA.
DR   RefSeq; WP_011517930.1; NC_007973.1.
DR   AlphaFoldDB; Q1LHJ8; -.
DR   SMR; Q1LHJ8; -.
DR   STRING; 266264.Rmet_3506; -.
DR   PRIDE; Q1LHJ8; -.
DR   EnsemblBacteria; ABF10378; ABF10378; Rmet_3506.
DR   KEGG; rme:Rmet_3506; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_4; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000002429; 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..654
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_1000016656"
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   654 AA;  71749 MW;  5D91C285B4119178 CRC64;
     MLYPKEFDVI VVGGGHAGTE AALAAARMGC QTLLLSHNIE TLGQMSCNPS IGGIGKGHLV
     KEVDAMGGAM AAATDEAGIQ FRILNSSKGP AVRATRAQAD RVLYRKAIRT RLENQPNLML
     FQQAVDDLMV EGDRVVGART QVGIDFRARA VVLTAGTFLD GKIHVGLDNY TGGRAGDPAA
     VSLSARLKEL KLPQGRLKTG TPPRIDGRTI DFSVMEEQPG DLDPVPVFSF LGRPEQHPQQ
     LPCWITHTNS RTHDVIRGGL DRSPMYTGVI EGVGPRYCPS IEDKIHRFAS KESHQIFLEP
     EGLTTNEFYP NGISTSLPFD VQLELVHSIR GLENAHILRP GYAIEYDYFD PRGLKSSLES
     KAIEGLFFAG QINGTTGYEE AAAQGLLAGI NAGCYVRERD AWTPRRDQAY LGVLVDDLIT
     RGVTEPYRMF TSRAEFRLSL REDNADMRLT EIGRELGVVD DVRWDAFNRK RDAVSRETER
     LKSTWVNPTL LPEADAVPLL GKGIEREYSL ADLLRRPEVR YEALVALQDG RFAPETPLAD
     DTMLAEQIRE QIEIGIKYHG YIARQAAEVD KLEANESTKL PPNFDYTEVR GLGFEVSQKL
     NQHRPETLGQ ASRISGVTPA AISLLLVHLK KKGMGRAAAQ TSATPVAGNG QEAA