ID   MNMG_VEREI              Reviewed;         658 AA.
AC   A1WGT2;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 77.
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=Veis_1063;
OS   Verminephrobacter eiseniae (strain EF01-2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Verminephrobacter.
OX   NCBI_TaxID=391735;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EF01-2;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2.";
RL   Submitted (DEC-2006) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABM56839.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000542; ABM56839.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041949824.1; NC_008786.1.
DR   AlphaFoldDB; A1WGT2; -.
DR   SMR; A1WGT2; -.
DR   STRING; 391735.Veis_1063; -.
DR   EnsemblBacteria; ABM56839; ABM56839; Veis_1063.
DR   KEGG; vei:Veis_1063; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_4; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000000374; 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..658
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345358"
FT   BINDING         13..18
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         285..299
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   658 AA;  71930 MW;  6E7A9BC99F2DCBF3 CRC64;
     MLYPQEFDVI VVGAGHAGTE AALAAARLGQ RTLLLTQSLE TLGQMSCNPS IGGIGKGHLV
     KEVDALGGAM ALATDESGIQ FRILNRSKGP AVRATRAQAD RLLYKAAIRR RLENQPGLWL
     FQQAVDDLML EGDRVVGAVT QVGVVFCARA VVLTAGTFLD GKIHVGLSHY AAGRAGEPSA
     IGLSARLKEL KLPQGRLKTG TPPRIDGRSI DWSQCEEQPG DGMPGGVNAG QVPVFSFMAH
     AYGGARMHPQ QLPCWITHTN QRTHAIIRSG FDRSPMFTGS IEGVGPRYCP SVEDKINRFA
     DKDSHQVFLE PEGLGTHEVY PNGISTSLPF DIQYQLVRSM AGLENAHILR PGYAIEYDYF
     DPRALKSNFE TRQIRGLFFA GQINGTTGYE EAAAQGLFAG VNAALQCRGD APWLPGRDQA
     YLGVLVDDLI TKGVTEPYRM FTSRAEFRLQ LREDNADMRL TEVGRRMGLV DDARWEVFSR
     KRDAVLRETE RLKATWVNPR NLPDIESGRV LGKPMAHEYS LFELLRRPDV DYAGLMSLDG
     GKYAAADVSR ETLGMLSESV VEQVEIAAKY AGYIERQKGE VERAAHFETL RLPAGLDYAQ
     VTALSIEARQ VLSRHRPETL GQASRITGIT PAAISLLLVH LKKGGFKGFM SANADAQA