ID   MNMG_THET8              Reviewed;         597 AA.
AC   Q5SGV8;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=TTHA1972;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) 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}.
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DR   EMBL; AP008226; BAD71795.1; -; Genomic_DNA.
DR   RefSeq; WP_011229056.1; NC_006461.1.
DR   RefSeq; YP_145238.1; NC_006461.1.
DR   AlphaFoldDB; Q5SGV8; -.
DR   SMR; Q5SGV8; -.
DR   STRING; 300852.55773354; -.
DR   EnsemblBacteria; BAD71795; BAD71795; BAD71795.
DR   GeneID; 3169842; -.
DR   KEGG; ttj:TTHA1972; -.
DR   PATRIC; fig|300852.9.peg.1943; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_0; -.
DR   OMA; FRPGYAI; -.
DR   PhylomeDB; Q5SGV8; -.
DR   Proteomes; UP000000532; 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   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..597
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000117204"
FT   BINDING         10..15
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         267..281
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   597 AA;  65202 MW;  D5DE0C2763EA19B3 CRC64;
     MAGYDVVVVG GGHAGLEAAW AAAALGVRVA LVTVNPDRIG MMPCNPAVGG PGKSQLVAEV
     VALGGLMGRA ADAAAIHTRV LNRSKGPAVQ SLRVQVDRDL YALKAQEILA ERPVEVLRGE
     VAALWVEGGR LLGVRTVDGR TLPAKAVVVA GGTFLSGVVW YGRKSRPAGR QGEPPARFLS
     QSLKAVGHTL RRFKTGTPPR IRADSVDFGR LEVVPPEVPP GSFTGNPGPH AARLPTWQTR
     TTARTHRLIR ENLHLSPLYA GDIQGIGPRY CPSIEDKVVR FADKESHLLF VEPDGLSTTE
     VYLQGFSSSL PPELQEEMVR SLPGFERAVI QRYAYAVEYD SLDPTELTRG LQSRLLPGLF
     SAGQVNGTSG YEEAAAQGLL AGLNAARFAL GLPEVHLPRE SGYIGVLVDD LVGRGTDEPY
     RMMTSRVELR LLCRADNADE RLTPLAVAWG LRPKEDLERV EAKYRRVAAE LRRLQALRVE
     GVSGLQWLRR PENTYRALAE RFPPSEPLSP EEAYQVEVRA KYAGYIERQE RLREKMKDLE
     AFRIPEGMDF PKVPGLSREA AEKLSRHRPK SLAEAARIPG VRDSDLTALA VHLRRGA