ID   MNMG_NEIM0              Reviewed;         628 AA.
AC   A9M3R4;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
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=NMCC_1957;
OS   Neisseria meningitidis serogroup C (strain 053442).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=374833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=053442;
RX   PubMed=18031983; DOI=10.1016/j.ygeno.2007.10.004;
RA   Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X., Xiong Z.,
RA   Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y., Shao Z.,
RA   Liang X., Xu J., Jin Q.;
RT   "Characterization of ST-4821 complex, a unique Neisseria meningitidis
RT   clone.";
RL   Genomics 91:78-87(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABX74082.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000381; ABX74082.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A9M3R4; -.
DR   SMR; A9M3R4; -.
DR   EnsemblBacteria; ABX74082; ABX74082; NMCC_1957.
DR   KEGG; nmn:NMCC_1957; -.
DR   HOGENOM; CLU_007831_2_2_4; -.
DR   Proteomes; UP000001177; 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..628
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345305"
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   628 AA;  69769 MW;  F738DDF6C69378D2 CRC64;
     MIYPKTYDVI VVGGGHAGTE AALAAARMGA QTLLLTHNIE TLGQMSCNPS IGGIGKGHLV
     RELDALGGAM ALATDKSGIQ FRRLNASKGA AVRATRAQAD RILYKAAIRE MLENQENLDL
     FQQAVEDVTL DGDRISGVIT AMGVEFKARA VVLTAGTFLS GKIHIGLENY EGGRAGDPAA
     KSLGGRLREL KLPQGRLKTG TPPRIDGRTI DFSQLTEQPG DTPVPVMSVR GNAEMHPRQV
     SCWITHTNTQ THDIIRSGFD RSPMFTGKIE GVGPRYCPSI EDKINRFADK DSHQIFLEPE
     GLTTHEYYPN GISTSLPFDI QIALVRSMKG LENAHILRPG YAIEYDYFDP RNLKASLETK
     TIQGLFFAGQ INGTTGYEEA AAQGLLAGAN AVQYVREQDP LLLRREQAYL GVLVDDLITK
     GVNEPYRMFT SRAEYRLQLR EDNADMRLTE DGYKIGLVGE EQWRMFNEKR EAIEREIQRL
     KTTWYTPQKL AEDEQIRVFG QKLSREANLH DLLRRPNLDY AALMTLEGAM PSENLSAEVI
     EQVEIQVKYQ GYIDRQNEEI DSRRDIETLK LPDDIDYSKV KGLSAEVQQK LNQHKPETVG
     QASRISGVTP AAVALLMVHL KRGFKDAK