ID   MNMG_STAA3              Reviewed;         625 AA.
AC   Q2FDE9;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 83.
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=SAUSA300_2645;
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=367830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300;
RX   PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABD20531.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000255; ABD20531.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000249662.1; NZ_CP027476.1.
DR   AlphaFoldDB; Q2FDE9; -.
DR   SMR; Q2FDE9; -.
DR   PRIDE; Q2FDE9; -.
DR   EnsemblBacteria; ABD20531; ABD20531; SAUSA300_2645.
DR   KEGG; saa:SAUSA300_2645; -.
DR   HOGENOM; CLU_007831_2_2_9; -.
DR   Proteomes; UP000001939; 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..625
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345339"
FT   BINDING         11..16
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         123
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         178
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         270..284
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         367
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   625 AA;  70116 MW;  27CA7DD9B0C99BD9 CRC64;
     MVQEYDVIVI GAGHAGVEAG LASARRGAKT LMLTINLDNI AFMPCNPSVG GPAKGIVVRE
     IDALGGQMAK TIDKTHIQMR MLNTGKGPAV RALRAQADKV LYQQEMKRVI EDEENLHIMQ
     GMVDELIIED NEVKGVRTNI GTEYLSKAVI ITTGTFLRGE IILGNMKYSS GPNHQLPSIT
     LSDNLRELGF DIVRFKTGTP PRVNSKTIDY SKTEIQPGDD VGRAFSFETT EYILDQLPCW
     LTYTNAETHK VIDDNLHLSA MYSGMIKGTG PRYCPSIEDK FVRFNDKPRH QLFLEPEGRN
     TNEVYVQGLS TSLPEHVQRQ MLETIPGLEK ADMMRAGYAI EYDAIVPTQL WPTLETKMIK
     NLYTAGQING TSGYEEAAGQ GLMAGINAAG KVLNTGEKIL SRSDAYIGVL IDDLVTKGTN
     EPYRLLTSRA EYRLLLRHDN ADLRLTDMGY ELGMISEERY ARFNEKRQQI DAEIKRLSDI
     RIKPNEHTQA IIEQHGGSRL KDGILAIDLL RRPEMTYDII LELLEEEHQL NADVEEQVEI
     QTKYEGYINK SLQQVEKVKR MEEKKIPEDL DYSKIDSLAT EAREKLSEVK PLNIAQASRI
     SGVNPADISI LLIYLEQGKL QRVSD