ID   MNMG_TREPS              Reviewed;         630 AA.
AC   B2S1Z2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=TPASS_0044;
OS   Treponema pallidum subsp. pallidum (strain SS14).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=455434;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS14;
RX   PubMed=18482458; DOI=10.1186/1471-2180-8-76;
RA   Matejkova P., Strouhal M., Smajs D., Norris S.J., Palzkill T.,
RA   Petrosino J.F., Sodergren E., Norton J.E., Singh J., Richmond T.A.,
RA   Molla M.N., Albert T.J., Weinstock G.M.;
RT   "Complete genome sequence of Treponema pallidum ssp. pallidum strain SS14
RT   determined with oligonucleotide arrays.";
RL   BMC Microbiol. 8:76-76(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}.
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DR   EMBL; CP000805; ACD70471.1; -; Genomic_DNA.
DR   RefSeq; WP_010881493.1; NC_021508.1.
DR   AlphaFoldDB; B2S1Z2; -.
DR   SMR; B2S1Z2; -.
DR   PRIDE; B2S1Z2; -.
DR   EnsemblBacteria; ACD70471; ACD70471; TPASS_0044.
DR   GeneID; 57878585; -.
DR   KEGG; tpp:TPASS_0044; -.
DR   PATRIC; fig|455434.6.peg.40; -.
DR   OMA; FRPGYAI; -.
DR   Proteomes; UP000001202; 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_1000095668"
FT   BINDING         14..19
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         282..296
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   630 AA;  70176 MW;  1B52C6F02C1EC275 CRC64;
     MGFRFSDYDV IVVGGGHAGA EAALAAARMG EHTLLITQTI DSIGRLSCNP SIGGISKGNI
     VREIDALGGE MGKFADACMI QYRLLNKSRG PAVQAPRIQA DKFLYAQKVK YTLECTQHLH
     LYQDTVVDVV CSNTTDAGYV AYGAAHAVVT ARGRRISARA VVLTTGTFME GRVYIGEYEA
     PEGRLGEHAA EGLGAALRKK GFQMGRLKTG TPARVLRKSV DLSVMEKQEA DAIMRPFSFA
     HVEINRPHAD CYINYTNERT HQLIRENFHR SPFFSGRIKA VGTRYCPSIE DKVRKFPDRI
     RHQLYIEPEG LDTEELYING LSSCLPEDIQ DEMIRTIPGM ERAVITRPAY AVDYAVLFPV
     QLGIDLQTKR VSGLFSAGQI NGTSGYEEAG GQGIIAGINA ALYARSTKTK EEYHPFVLKR
     DEAYIGVMID DLVTQGIDEP YRMFTARAEY RLKLRHDTAD ERLTEKAYAI GLQKKSAVET
     LQKKMRTKHE ILHLLQTNKV SLTHANAYVQ LKPHIGKSFA ATLRDPVIPL GLIASLNEQI
     AQFPLEVFQS VGVEIRYEHY IAAQDQRIAQ VEKMEGIKIP AHFDYARISG LSVESRTRLE
     HVRPDTIGQV GRMRGIRPSD VMLLLAHLKR