ID   MNMG_LIGS1              Reviewed;         637 AA.
AC   Q1WVH6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=LSL_0124;
OS   Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=362948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCC118;
RX   PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA   Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA   Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA   Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT   "Multireplicon genome architecture of Lactobacillus salivarius.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006).
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; CP000233; ABD98941.1; -; Genomic_DNA.
DR   RefSeq; WP_003700792.1; NC_007929.1.
DR   RefSeq; YP_535024.1; NC_007929.1.
DR   AlphaFoldDB; Q1WVH6; -.
DR   SMR; Q1WVH6; -.
DR   STRING; 362948.LSL_0124; -.
DR   PRIDE; Q1WVH6; -.
DR   EnsemblBacteria; ABD98941; ABD98941; LSL_0124.
DR   KEGG; lsl:LSL_0124; -.
DR   PATRIC; fig|362948.14.peg.198; -.
DR   HOGENOM; CLU_007831_2_2_9; -.
DR   OMA; FRPGYAI; -.
DR   Proteomes; UP000006559; 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..637
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_1000016616"
FT   BINDING         18..23
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         281..295
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   637 AA;  71228 MW;  A35F2CDF3C5EA338 CRC64;
     MEFGKRYKAK DYDVIVVGAG HAGCEAALAS ARMGNETLLI TINLEMVAFM PCNPSIGGPA
     KGIVVREIDA MGGEMGRNID KTYVQMRMLN TGKGPAVRAL RAQADKRQYS IEMKHTIEQT
     PHLTLRQGIV DDLIIEDGEV KGVVTNTGAC YGAKSVVLTT GTAARGKIII GELMYSSGPN
     NTQPALELSK NLAKLGFELK RFKTGTPPRV DGNTIDYDKT EEQPGDVEPN HFSYESKDED
     YLKVKDQLSC WLTYTNEYTH KIIQDNLDRA PMFTGVIEGV GPRYCPSIED KIVRFSDKPR
     HQLFLEPEGR NTDEYYVQGL STSLPEEVQQ EMVRSIDGLE HAEMMRPGYA IEYDVVSPYQ
     LRPTLETKLI KGLYTAGQTN GTSGYEEAAG QGFIAGVNAG RRAKGLEEIT LKRSDAYIGV
     MIDDLVTKGT NEPYRLLTSR AEYRLILRHD NADLRLTELG HEIGLISDER YAAFEEKKAQ
     IEAEKQRLSK IRIKPNAEVN AFVEAHGDRE LKDGVLATEF LRRPYVTYQD LLKFIPAPAE
     PLDRRVIEQI EIQFKYEGYI KKEYAKVEKL KRMEAKKIPA RIDYSRIEGI ATEAQQKLAK
     IQPETLAQAG RISGVNPADL SILAVYIEQG KIARVDD