MNMG_TREDE
ID MNMG_TREDE Reviewed; 628 AA.
AC Q73PH1;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=TDE_0828;
OS Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS / KCTC 15104).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA Seshadri R., Myers G.S.A., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA Ren Q., Brinkac L.M., Madupu R., Kolonay J.F., Durkin S.A., Daugherty S.C.,
RA Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G.,
RA Malek J.A., Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K.,
RA Pal S., Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E.,
RA Baca E., Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT "Comparison of the genome of the oral pathogen Treponema denticola with
RT other spirochete genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
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; AE017226; AAS11319.1; -; Genomic_DNA.
DR RefSeq; NP_971438.1; NC_002967.9.
DR RefSeq; WP_002682089.1; NC_002967.9.
DR AlphaFoldDB; Q73PH1; -.
DR SMR; Q73PH1; -.
DR STRING; 243275.TDE_0828; -.
DR EnsemblBacteria; AAS11319; AAS11319; TDE_0828.
DR GeneID; 2739512; -.
DR KEGG; tde:TDE_0828; -.
DR PATRIC; fig|243275.7.peg.797; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_12; -.
DR OMA; FRPGYAI; -.
DR OrthoDB; 146811at2; -.
DR Proteomes; UP000008212; 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_0000117205"
FT BINDING 13..18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 281..295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 628 AA; 70228 MW; 020D7F82D70F4CDC CRC64;
MYRFSDYDVI VVGAGHAGIE AALASARMGE AVLLITQTLD SAGRLSCNPS IGGISKGNIV
REIDALGGEM GKLADASMIQ YRLLNKSRGP AVQAPRVQAD KFLYSQLAKH AIELEKNLHV
FQDTVIDIVS SNTNESGYVE KGSVQYVKTE RGREFSAKAV VLATGTFMEG KIYIGEYESP
DGRLGERAAI GLGPALAKKG FTVGRLKTGT PMRILRRSFD SSLTEEQEAD EIMRPFSFSN
AEIHRPYAKC YITHTNQETH DIIRENLHRA ALFSGKITGT GARYCPSIED KIKKFPERDR
HHVYIEPEGL NTEELYINGL SSSLPEDVQD RMIRTIPCFK DVIITRPAYA VDYAYVSPIQ
LSSDLQTRRI EGLFLAGQIN GTSGYEEAGG QGIIAGINAA LFSRSLKFKD EKYVPFVLKR
DEAYIGVMID DLVTQGVDEP YRMFTARAEY RLNLRHDTAD ERLTERAYQI GLQTKEASNR
LKEKLLTREK IISLWKDIKI TRDLIAKNPE LKNHIGKSLA DALHDPQVSL ECICAIDENS
KDYSAELLES AELEIRYEHY IAVQNRKIAK VKRMENTKIP ADFDYDAVSG LSTESRTRLK
EVRPETIGQA SRIRGIRPSD IMLLSILL