ID   MNMG_DESHD              Reviewed;         637 AA.
AC   B8G0L2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=Dhaf_4956;
OS   Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=272564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10664 / DCB-2;
RX   PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA   Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA   Tiedje J.M.;
RT   "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT   anaerobe capable of dehalogenation and metal reduction.";
RL   BMC Microbiol. 12:21-21(2012).
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; CP001336; ACL22948.1; -; Genomic_DNA.
DR   RefSeq; WP_015945542.1; NC_011830.1.
DR   AlphaFoldDB; B8G0L2; -.
DR   SMR; B8G0L2; -.
DR   EnsemblBacteria; ACL22948; ACL22948; Dhaf_4956.
DR   KEGG; dhd:Dhaf_4956; -.
DR   HOGENOM; CLU_007831_2_2_9; -.
DR   OMA; FRPGYAI; -.
DR   Proteomes; UP000007726; 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; tRNA processing.
FT   CHAIN           1..637
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_1000122744"
FT   BINDING         14..19
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   637 AA;  70487 MW;  987560BE7C28DAEF CRC64;
     MEYLAGNYDV IVVGAGHAGC EAALAAARMG GRTLLITLSL DNIAHMDCNP SLGGPAKGHL
     VREIDALGGQ MGITADETSL QVRMLNTGKG PAVHALRIQS DKQAYHLHMR NAILGQENLV
     LHQALVERIK TEDGKVSGVV TRTGAFYAAP NVILTSGTYL RGRIIIGDTM YEGGPNGQQT
     AMNLSGALKE LGLELGRFKT GTPPRIHRRS VDYTKFTVQP GDSVPWRYSF MPTQSMFWGR
     DVDKQIPCWL GYTTPETHQI IQDNIHRAPL YSGKIEGIGP RYCPSIEDKV VRFADRPTHQ
     IFLEPEGWNS DELYMAGLST SMPEEIQYDI IHSIPGLEKA ELLRPGYAIE YDYVKPYQLS
     LSLEVRKIPG LFTAGQLNGT SGYEEAAAQG LLAGINAALR VQGKEPFIVR RSEGYLGVLI
     DDLVNKGVKE PYRLLTSRAE YRLILRQDNA DLRLTPRGRE IGLVKDERWA AFQKKKAAIA
     EINALWRGTT FSPLNEHLAE VLAGVHSAPV HGGISGEELM RRPEITINEI KQLIPQLAEY
     DEEALLEAGI EIKYAGYIEK QLAEIERFAK MEERMIPEEI VYDQIKGLST EGRQRLKEVA
     PANMGQATRI TGVTPADISV LLVYLEQKRR GGQIHAT