ID   MNMG_RICTY              Reviewed;         621 AA.
AC   Q68XT0;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
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}; OrderedLocusNames=RT0076;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU03562.1; -; Genomic_DNA.
DR   RefSeq; WP_011190549.1; NC_006142.1.
DR   AlphaFoldDB; Q68XT0; -.
DR   SMR; Q68XT0; -.
DR   STRING; 257363.RT0076; -.
DR   EnsemblBacteria; AAU03562; AAU03562; RT0076.
DR   KEGG; rty:RT0076; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_5; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000000604; 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..621
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000117167"
FT   BINDING         10..15
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         122
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         177
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         269..283
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         366
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   621 AA;  69134 MW;  5AC5B7DE978FD61C CRC64;
     MLKYGVIIIG GGHAGVEAAA ASARLGVHTL LITLKPENLG EMSCNPAIGG IAKGTLVKEI
     DALDGLMGFV IDKAGIHYKM LNETRGPAVW GPRAQADRKL YKKVMYQILT NYRNLDILYG
     KVEDIQIKSS KVEAVILNNG IKIFCQKVVL TTGTFLSGFI HIGSMKIPAG RIYEEPSYGL
     SNTLKRLGFK IARLKTGTPP RIDGRTIDYS KTTLQQGDQI PRPFSELTDA IDVPQINCFI
     TKTTAETHDI IRENLDKSAM YSGQIKGIGP RYCPSIEDKI VKFSTKLEHR IFLEPEGLED
     YTIYPNGIST SLPKEIQYKL IKTIPGLENA QVLRPGYAIE YDYVDPREIN ITLETKKITG
     LYFAGQINGT TGYEEAAGQG IIAGINAALS VKDQEPFILT RATSYIGVMI DDLTTSGTVE
     PYRMFTSRSE YRLSLRADNA DLRLTELGIN IGVVTEKRKN IFTKKCNNIE KTKLLLNKLS
     LTTSKLAKIG IQVAQDGKYK TVLDLFKIPT FNVEQAIKIF PILRKQNNNI LQLLYIEAKY
     ASYLTRQYAD INLFQSEEIQ LIPKNIDYFK IPSISLEIQE KLSYHKPTTI GVARRISGIT
     PAAIMAIIIY LKTKYSDGSS K