ID   MNMG_NEIG1              Reviewed;         628 AA.
AC   Q5F5Y0;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
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}; OrderedLocusNames=NGO1788;
OS   Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=242231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700825 / FA 1090;
RA   Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA   Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA   Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA   Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT   "The complete genome sequence of Neisseria gonorrhoeae.";
RL   Submitted (MAR-2003) 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}.
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DR   EMBL; AE004969; AAW90407.1; -; Genomic_DNA.
DR   RefSeq; YP_208819.1; NC_002946.2.
DR   AlphaFoldDB; Q5F5Y0; -.
DR   SMR; Q5F5Y0; -.
DR   STRING; 242231.NGO_1788; -.
DR   EnsemblBacteria; AAW90407; AAW90407; NGO_1788.
DR   KEGG; ngo:NGO_1788; -.
DR   PATRIC; fig|242231.10.peg.2146; -.
DR   HOGENOM; CLU_007831_2_2_4; -.
DR   OMA; FRPGYAI; -.
DR   Proteomes; UP000000535; 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..628
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000117139"
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;  69624 MW;  71AE232546B197F1 CRC64;
     MIYPKTYDVI VVGGGHAGTE AALAAARMGA QTLLLTHNIE TLGQMSCNPS IGGIGKGHLV
     RELDALGGAM ALATDKSGIQ FRRLNASKGA AVRATRAQAD RILYKASIRE MLENQENLDL
     FQQAVEDVTL EGERISGVIT AMGVEFKARA VVLTAGTFLS GKIHIGLENY EGGRAGDPAA
     KSLGGRLREL KLPQGRLKTG TPPRIDGRTI DFSQLTEQPG DTPVPVMSVR GNAEMHPRQV
     SCWITHTNTQ THDIIRSGFD RSPMFTGKIE GVGPRYCPSI EDKINRFADK DSHQIFLEPE
     GLTTHEYYPN GISTSLPFDI QIALVRSMKG LENAHILRPG YAIEYDYFDP RNLKASLETK
     TIEGLFFAGQ INGTTGYEEA AAQGLLAGAN AVQYVRGQDP LLLRREQAYL GVLVDDLITK
     GLNEPYRMFT SRAEYRLQLR EDNADMRLTE DGYKIGLVGE AQWRMFNEKR EAVEREIQRL
     KTTWYTPQKL AEDEQIRVFG QKLSREANLH DLLRRPNLDY AALMTLEGAM PSENLSAEVI
     EQVEIQVKYQ GYIDRQNEEI DSRRDIETLK LPDGIDYGRV KGLSAEVQQK LNQHKPETVG
     QASRISGVTP AAVALLMVHL KRGFKDAK