ID   MNMG_FLAJ1              Reviewed;         623 AA.
AC   A5FL86;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=Fjoh_1003;
OS   Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS   14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=376686;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 / UW101;
RX   PubMed=19717629; DOI=10.1128/aem.01495-09;
RA   McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA   Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA   Cheng Y.Q., Stein J.L.;
RT   "Novel features of the polysaccharide-digesting gliding bacterium
RT   Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL   Appl. Environ. Microbiol. 75:6864-6875(2009).
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; CP000685; ABQ04036.1; -; Genomic_DNA.
DR   RefSeq; WP_012023089.1; NZ_MUGZ01000034.1.
DR   AlphaFoldDB; A5FL86; -.
DR   SMR; A5FL86; -.
DR   STRING; 376686.Fjoh_1003; -.
DR   PRIDE; A5FL86; -.
DR   EnsemblBacteria; ABQ04036; ABQ04036; Fjoh_1003.
DR   KEGG; fjo:Fjoh_1003; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_10; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000006694; 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..623
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345272"
FT   BINDING         12..17
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         272..286
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   623 AA;  69962 MW;  EF43DE59994F9902 CRC64;
     MFLEEYDVIV VGAGHAGSEA AAAAANLGSK TLLVTMSLQN IAQMSCNPAM GGIAKGQIVR
     EIDALGGYSG IVSDRTAIQF KMLNKSKGPA MWSPRVQSDR MRFAEEWRMM LEGTPNLDFY
     QEMVKGLIIE NGKIKGIRTS LGVEIRSKSV VLTNGTFLNG LIHIGEKQFG GGRAGESAAT
     GITEDLVKAG FEAGRMKTGT PPRVDGRSLD YSKMNEEKGD AKPDKFSYSD LTKPLTQQRS
     CYMTYTSLNV HDILREGFDR SPMFNGRIKS LGPRYCPSIE DKINRFADKE RHQLFVEPEG
     WNTCEVYVNG FSTSLPEDIQ FKALRSVAGF ENVKFFRPGY AIEYDYFPPT QLKHTLETKL
     VEGLYFAGQI NGTTGYEEAA SQGLMAGINA HLKVHEKAPL ILKRDEAYIG VLIDDLITKG
     TEEPYRMFTS RAEYRTLLRQ DNADFRLTPM SFEIGLASED RMRRMEHKLN ESEKMVAFFK
     ETSVTVAETN PILIEKESAP ISQGDKMFKV FSRPQIELED MLKFEKVDSY IKENNLDEEI
     VEQAVIQVKY SGYIEKERNN ADKLNRLEEV KIPENFDYNK IKSMSIEAKQ KLSKIRPVTI
     SQASRISGVS PSDISVLLIY MGR