ID   MNMG_DELAS              Reviewed;         659 AA.
AC   A9BQJ1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 84.
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=Daci_0046;
OS   Delftia acidovorans (strain DSM 14801 / SPH-1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=398578;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT   "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL   Submitted (NOV-2007) 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; Evidence={ECO:0000255|HAMAP-
CC         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; CP000884; ABX32693.1; -; Genomic_DNA.
DR   RefSeq; WP_012201986.1; NC_010002.1.
DR   AlphaFoldDB; A9BQJ1; -.
DR   SMR; A9BQJ1; -.
DR   STRING; 398578.Daci_0046; -.
DR   GeneID; 24115771; -.
DR   KEGG; dac:Daci_0046; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_4; -.
DR   Proteomes; UP000000784; 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; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 1.10.150.570; GidA associated domain, C-terminal subdomain; 1.
DR   Gene3D; 1.10.10.1800; tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG/GidA; 1.
DR   HAMAP; MF_00129; MnmG_GidA; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR049312; GIDA_C_N.
DR   InterPro; IPR004416; MnmG.
DR   InterPro; IPR002218; MnmG-rel.
DR   InterPro; IPR020595; MnmG-rel_CS.
DR   InterPro; IPR026904; MnmG_C.
DR   InterPro; IPR047001; MnmG_C_subdom.
DR   InterPro; IPR044920; MnmG_C_subdom_sf.
DR   InterPro; IPR040131; MnmG_N.
DR   NCBIfam; TIGR00136; gidA; 1.
DR   PANTHER; PTHR11806; GLUCOSE INHIBITED DIVISION PROTEIN A; 1.
DR   PANTHER; PTHR11806:SF0; PROTEIN MTO1 HOMOLOG, MITOCHONDRIAL; 1.
DR   Pfam; PF01134; GIDA; 1.
DR   Pfam; PF13932; GIDA_C; 1.
DR   Pfam; PF21680; GIDA_C_1st; 1.
DR   SMART; SM01228; GIDA_assoc_3; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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..659
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_1000095649"
FT   BINDING         13..18
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         281..295
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   659 AA;  72631 MW;  765C932EFD07B1CE CRC64;
     MLYPQEFDVI VVGGGHAGTE AALAAARMGC RTLLLSHNIE TLGQMSCNPS IGGIGKGHLV
     KEVDALGGAM ALATDIGGIQ FRILNSSKGP AVRATRAQAD RILYKAAIRD MLENQPNLWL
     FQQAVDDLMV EGDRVVGAVT QVGVRFRSRT VVLTAGTFLD GKIHVGLNNY AAGRAGDPPA
     VSLSSRLKEL QLPQGRLKTG TPPRLDGRSI DFSQCEEQPG DGMPGGVNEG VLPVFSFIGN
     AAMHPRQMPC WITHTNERTH DIIRSGFDRS PMFTGKIEGV GPRYCPSVED KINRFADKES
     HQIFLEPEGL TTNEFYPNGI STSLPFDIQY ELVRSMKGLE NAHILRPGYA IEYDYFDPRS
     LKSSFETRQI QGLFFAGQIN GTTGYEEAAA QGLFAGLNAA LQCRGQEAWL PRRDEAYLGV
     LVDDLITKGV TEPYRMFTSR AEFRLQLRED NADMRLTEAG RAMGLVDDAR WDAFSRKRDA
     VSRETERLKS TWVNPRIVTP EESERVLGKS IEREYNLFDL LRRPDVGYGK LMSLNEGRYA
     SADVQPDVLG DLSASVVEQV EIAAKYAGYI DRQKDEVQRA AHFENLRLPA ELDYMQVPAL
     SFEVRQSLQK HRPETLGQAS RMSGVTPAAI SLLMVHLKKG GFRGFAPDVT DAKGEEASA
//