ID   MNMG_BURMS              Reviewed;         657 AA.
AC   A1V8U3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=BMASAVP1_A3367;
OS   Burkholderia mallei (strain SAVP1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320388;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAVP1;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
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; CP000526; ABM49638.1; -; Genomic_DNA.
DR   RefSeq; WP_004195816.1; NC_008785.1.
DR   AlphaFoldDB; A1V8U3; -.
DR   SMR; A1V8U3; -.
DR   GeneID; 56593908; -.
DR   KEGG; bmv:BMASAVP1_A3367; -.
DR   HOGENOM; CLU_007831_2_2_4; -.
DR   OMA; FRPGYAI; -.
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..657
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_1000016565"
FT   REGION          636..657
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         13..18
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         274..288
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   657 AA;  71981 MW;  E75CD490ADDDE67E CRC64;
     MLYPTEFDVI VVGGGHAGTE AALASARMGA KTLLLTHNIE TLGQMSCNPS IGGIGKGHLV
     KEVDALGGAM AAATDEGGIQ FRILNSSKGP AVRATRAQAD RVLYKQAIRR RLENQPNLWL
     FQQAVDDLMV EGDRVVGAVT QVGVRFRARA VVLTAGTFLD GKIHVGLNHY TGGRAGDPAA
     VSLSSRLKEL NLPQGRLKTG TPPRIDGRTI DFSKLDEQPG DLDPIPVFSF LGRAEQHPQQ
     LPCWVTHTNE RTHDIIRSGL DRSPMYTGVI EGVGPRYCPS IEDKIHRFAS KDSHQIFLEP
     EGLTTNEFYP NGISTSLPFD VQLALVHSMR GLEQAHILRP GYAIEYDYFD PRALKSSLET
     KAIGGLFFAG QINGTTGYEE AAAQGLLAGI NAGRYAQEKD AWCPRRDQAY LGVLVDDLVT
     RGVSEPYRMF TSRAEYRLSL REDNADMRLT EIGRELGVVD DVRWDAFNRK RDAVSRETER
     LRTTWVTPKT LPADEATALL GKPIDHEYSL AELLRRPGVS YDGVCGLRGG ECGPSEPLAE
     DELLLAQIKE QIEIGIKYQG YIERQAGEIE RNGANENTRL PDGIDYTEVR GLSFEVSQKL
     NQFRPETIGQ ASRISGMTPA AISLLMVHLK KRGLGRRKGA DSVPGADVQA DNTAAQQ