ID   MNMG_TRIEI              Reviewed;         637 AA.
AC   Q110Q9;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Tery_2841;
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Trichodesmium.
OX   NCBI_TaxID=203124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Richardson P.;
RT   "Complete sequence of Trichodesmium erythraeum IMS101.";
RL   Submitted (JUN-2006) 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;
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000393; ABG52015.1; -; Genomic_DNA.
DR   RefSeq; WP_011612376.1; NC_008312.1.
DR   AlphaFoldDB; Q110Q9; -.
DR   SMR; Q110Q9; -.
DR   STRING; 203124.Tery_2841; -.
DR   PRIDE; Q110Q9; -.
DR   EnsemblBacteria; ABG52015; ABG52015; Tery_2841.
DR   KEGG; ter:Tery_2841; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_3; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
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..637
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345356"
FT   BINDING         17..22
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         278..292
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   637 AA;  71659 MW;  0591A0D1EA41A250 CRC64;
     MNQTFDFQDE YDIIVVGAGH SGCEAALATA RLGCHTLLLT LNLDKIAWQP CNPAVGGPAK
     SQLTHEVDAL GGEIGKMADR TYLQKRILNS SRGPAVWALR AQTDKREYAT IMRNIVENQE
     NLRVRESMVT DLVLGDNEEI IGVETYFGVA FKCKAVILTT GTFLGGVIWV GNKSMPAGRA
     GEFSAIGLSE TLNKLGFETG RLKTGTPARV DKRSVDYTDL EAQPGDEKVR WFTFDPEVWV
     EREQMCCYLT RTTPETHKLI RDNLHLSPVY GGWVDAKGPR YCPSIEDKIV RFADKHSHQI
     FIEPEGRDIP ELYIQGFSTG LPEKLQLQML QSLPGLENCL MLRPAYAVEY DYLPATQCYP
     TLMTKKIEGL FCAGQINGTT GYEEAAAQGL VAGINAVKFV KNEEMIIFPR EQSYIGTLID
     DLCTKDLREP YRMLTSRSEY RLILRSDNAD QRLTPLGREI GLIDDRRWEL FESKQANINS
     EKSRLNSTRI KELDEVAINI VADTHTKIKG SITLADLLRR PGFHYVDLEK YNLGNLDLKL
     VEKEGAEIDI KYSGYLQRQQ NQIDQISRQK NRRLPTNLDY LSISTLSLEA REKLSKVQPL
     TIGQASRIGG VNPADINALL VYLEVQYRQF QLTSANV