ID   MNMG_ACTP7              Reviewed;         630 AA.
AC   B3H2Q2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=APP7_1717;
OS   Actinobacillus pleuropneumoniae serotype 7 (strain AP76).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=537457;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP76;
RA   Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N.,
RA   Tegetmeyer H., Singh M., Gerlach G.F.;
RT   "Genome and proteome analysis of A. pleuropneumoniae serotype 7.";
RL   Submitted (JUN-2008) 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; CP001091; ACE62369.1; -; Genomic_DNA.
DR   RefSeq; WP_005618124.1; NC_010939.1.
DR   AlphaFoldDB; B3H2Q2; -.
DR   SMR; B3H2Q2; -.
DR   EnsemblBacteria; ACE62369; ACE62369; APP7_1717.
DR   KEGG; apa:APP7_1717; -.
DR   HOGENOM; CLU_007831_2_2_6; -.
DR   OMA; FRPGYAI; -.
DR   BioCyc; APLE537457:APP7_RS08920-MON; -.
DR   Proteomes; UP000001226; 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..630
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_1000095641"
FT   BINDING         13..18
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         273..287
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   630 AA;  70054 MW;  6226501BC1959959 CRC64;
     MIYHEIYDVI VVGGGHAGTE AALAPARMGL KTLLLTHNID TLGQMSCNPA IGGIGKGHLV
     KEIDAMGGLM AIAIDQAGIQ FRTLNSSKGP AVRATRAQAD RVLYRQAVRT ALENQPNLDI
     FQQEVVDILV ENNRAVGAVT KMRLTFKARS VVLTAGTFLA GKIHIGLDNY AGGRAGDPAA
     TMLADRLRDL NLRIDRLKTG TPPRLDARTI NFDVLAKQHG DAELPVMSFM GSVDLHPRQI
     PCYITHTNEQ THDLIRNSLD RSPMYTGVIE GIGPRYCPSI EDKVMRFSDR NSHQIYLEPE
     GLSTIEVYPN GISTSLPFDV QMGIVNSMKG LEKTRIIKPG YAIEYDYFDP RDLKPTLETK
     AIEGLFFAGQ INGTTGYEEA AAQGLLAGIN AALQVQGKEA WFPTRDLAYT GVLVDDLCTL
     GTKEPYRVFT SRAEYRLLLR EDNADIRLTP IAHELGLIDD ARWARFNQKM ENIEREHERL
     KQIWIHPQSE HLAVVNELVN SPLTREASGE DLLRRPEVTY DKLTQVAAFA PALDDKQAAE
     QVEISIKYQG YIEHQQNEIE RHKRHENTLI PAEFDYDKVE SLSNEVRAKL MQHRPVSIGQ
     ASRISGITPA AISILLVNLK KQGMLKRGEL