ID   MNMG_POLSJ              Reviewed;         673 AA.
AC   Q12HF2;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Bpro_0073;
OS   Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas; unclassified Polaromonas.
OX   NCBI_TaxID=296591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS666 / ATCC BAA-500;
RX   PubMed=18723656; DOI=10.1128/aem.00197-08;
RA   Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA   Stothard P., Coleman N.V.;
RT   "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT   a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT   relevance to biotechnology.";
RL   Appl. Environ. Microbiol. 74:6405-6416(2008).
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; CP000316; ABE42040.1; -; Genomic_DNA.
DR   RefSeq; WP_011481050.1; NC_007948.1.
DR   AlphaFoldDB; Q12HF2; -.
DR   SMR; Q12HF2; -.
DR   STRING; 296591.Bpro_0073; -.
DR   EnsemblBacteria; ABE42040; ABE42040; Bpro_0073.
DR   KEGG; pol:Bpro_0073; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_4; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000001983; 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; Reference proteome; tRNA processing.
FT   CHAIN           1..673
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345316"
FT   BINDING         17..22
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         284..298
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   673 AA;  74027 MW;  22AA1F52519A4970 CRC64;
     MQSPYIYPQE FDVIVVGGGH AGTEAALASA RMGCKTLLLS HNIETLGQMS CNPSIGGIGK
     GHLVKEVDAM GGAMALATDE GGIQFRILNS SKGPAVRATR AQADRILYKA AIRRRLENQP
     NLWLFQQAVD DLMVEGDRVV GAVTQVGIRF RSRTVVLTAG TFLDGKIHVG LNNYAAGRAG
     DPPAVSLSSR LKELKLPQGR LKTGTPPRID GRTIDFSKCI EQPGDGMPGG TAGPVPVFSF
     MGGAIPHPQQ MPCWITHTNE RTHEIIRSGF DRSPMFTGKI DGVGPRYCPS VEDKINRFAD
     KESHQIFLEP EGLTTHEIYP NGISTSLPFD IQYELVRSMA GMENAHILRP GYAIEYDYFD
     PRALKTTFET RAIGGLFFAG QINGTTGYEE AAAQGMFAGI NAALQCRALG GLPNDHGGAW
     LPRRDEAYLG VLVDDLITKG VTEPYRMFTS RAEYRLMLRE DNADMRLTEK GRELGLVDDA
     RWDAFSRKRD AVSRETERLR SLWVNPHNLP LAEAERVLGK SIEREYNLLD LLRRPDVNYA
     GLMSLEEGKY ANPELAAEAA ASDDLAKSVI EQIEITAKYA GYIDLQKTEV ERAAHYENLK
     LPTDLDYLQV SALSFEARQT LARHRPETLG MASRISGITP ATVSLLLVHL KKNLWKNTVP
     LKTTDTSTEK AQA