ID   MNMG_POLNA              Reviewed;         667 AA.
AC   A1VIB1;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Pnap_0063;
OS   Polaromonas naphthalenivorans (strain CJ2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=365044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ2;
RX   PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA   Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT   "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT   tar-contaminated sediment, reveals physiological and metabolic versatility
RT   and evolution through extensive horizontal gene transfer.";
RL   Environ. Microbiol. 11:2253-2270(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; CP000529; ABM35389.1; -; Genomic_DNA.
DR   RefSeq; WP_011799499.1; NC_008781.1.
DR   AlphaFoldDB; A1VIB1; -.
DR   SMR; A1VIB1; -.
DR   STRING; 365044.Pnap_0063; -.
DR   EnsemblBacteria; ABM35389; ABM35389; Pnap_0063.
DR   KEGG; pna:Pnap_0063; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_4; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000000644; 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..667
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345315"
FT   BINDING         13..18
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         280..294
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   667 AA;  73249 MW;  925767FD122AB35F CRC64;
     MFYPQEFDVI VVGGGHAGTE AALAAARMGC KTLLLTHNIE TLGQMSCNPS IGGIGKGHLV
     KEVDAMGGAM ALATDEGGIQ FRILNGSKGP AVRATRAQAD RILYKAAIRR MIENQPNLWL
     FQQAVDDLMV EGDRVVGAVT QVGIKFRART VVLTAGTFLD GKIHVGLNNY PAGRAGDPPA
     VSLSARLKEL KLPQGRLKTG TPPRIDGRSI DFSKCGVQPG DGMPGGTPGP VPVFSFMGGN
     VPHPKQVPCW ITHTNERTHD IIRSGFDRSP MFTGKIDGVG PRYCPSVEDK INRFAGKDSH
     QIFLEPEGLT THEIYPNGIS TSLPFDIQYA LVRSMAGMEN AHILRPGYAI EYDYFDPRAL
     KTNFETRAIG GLFFAGQING TTGYEEAAAQ GMFAGINAAL QCQEKEAWLP KRDEAYLGVL
     VDDLITKGVT EPYRMFTSRA EFRLMLREDN ADMRLTEKGR ELGLVDDARW DAFNRKRDIV
     SRETQRLRAL WINPNNLPAS EAERVLGKAI EREYNLADLL RRPDVNYAGL MSLDGGRYAN
     PEIPTGNEDV SRETSTDSAL PADLVKSVIE QIEITAKYAG YIDLQKVEVE RASHYENLKL
     PADLDYLQVS ALSFEARQML SKHRPETLGL ASRIQGITPA TISLLLVHLK KNLWKNTTPL
     KSAEAEA