ID   MNMG_LEPBJ              Reviewed;         635 AA.
AC   Q04WG0;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=LBJ_0001;
OS   Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=355277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB197;
RX   PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA   Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA   Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA   Rood J.I., Davies J.K., Adler B.;
RT   "Genome reduction in Leptospira borgpetersenii reflects limited
RT   transmission potential.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(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; CP000350; ABJ74760.1; -; Genomic_DNA.
DR   RefSeq; WP_011669135.1; NC_008510.1.
DR   AlphaFoldDB; Q04WG0; -.
DR   SMR; Q04WG0; -.
DR   EnsemblBacteria; ABJ74760; ABJ74760; LBJ_0001.
DR   KEGG; lbj:LBJ_0001; -.
DR   HOGENOM; CLU_007831_2_2_12; -.
DR   OMA; FRPGYAI; -.
DR   Proteomes; UP000000656; Chromosome 1.
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.
PE   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; NAD; tRNA processing.
FT   CHAIN           1..635
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345290"
FT   BINDING         20..25
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         279..293
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   635 AA;  71795 MW;  9C402C0C102CC9BD CRC64;
     MIESKNQSFF PNRFDCVVVG AGHAGSEAAY IASKGGAKTL LITMNLDTIG QMSCNPAIGG
     IAKGHMVREV DALGGIMGKV IDNTGIQFKM LNTSKGPSVW APRAQAEKKE YQLKVKHTLE
     AEKNLSMRQD TVEELLIEND QVIGVKTGRG FEIYTNHVIL TTGTFLSSLV HIGTYQNENG
     RMCEPTVKGL SKSLAKYNLK LGRLKTGTPP RIHKNSVDLS VLAIQDGDAN PSPFSFSTEK
     ITRRQIPCYI TYTNVETHKL IHENLSLSPM YSGQIQSTGP RYCPSIEDKV VRFADRERHQ
     VFLEPEGYET TEIYLNGVST SLPEEVQWKL VRSLKGLENA EIVRPGYAIE YDYVDPTELK
     PTLETKKIKG LYHAGQINGT TGYEEAAAQG LVAAYSVLHS LKNLDPLLFK RSESYIGVLI
     DDLVYKGVED PYRMFTSRAE HRLLLRQDNA DQRLMKYGYE LGLVDQESYD RMKDKYERVN
     SVREKIYQIP LKPSDEFQNL LDQKGITNYK FGMKLDSFLK RPEIKIEDVE FMLPEVSSWS
     ESEKNILEME IKYEGYIKRE LETIQWKNKY LDLAIPEDIN YESIAGLKKE AIQKLKTHKP
     MTLEKAGQIS GVDPSDVDLL LYHIKGKRKQ EAEAS