MNMG_CLOAB
ID MNMG_CLOAB Reviewed; 626 AA.
AC Q97CW3;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=CA_C3733;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK81653.1; -; Genomic_DNA.
DR PIR; B97358; B97358.
DR RefSeq; NP_350313.1; NC_003030.1.
DR RefSeq; WP_010966993.1; NC_003030.1.
DR AlphaFoldDB; Q97CW3; -.
DR SMR; Q97CW3; -.
DR STRING; 272562.CA_C3733; -.
DR EnsemblBacteria; AAK81653; AAK81653; CA_C3733.
DR GeneID; 45000229; -.
DR KEGG; cac:CA_C3733; -.
DR PATRIC; fig|272562.8.peg.3923; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_9; -.
DR OMA; FRPGYAI; -.
DR OrthoDB; 146811at2; -.
DR Proteomes; UP000000814; 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..626
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_0000117087"
FT BINDING 15..20
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 626 AA; 70332 MW; 5E305114EE488CC6 CRC64;
MIKYFSGDYD VIVIGGGHAG CEAALAASRM GCRTLMCTMN LDSIAMMPCN PNIGGTAKGH
LVKEIDALGG EMGVNIDKTF IQSRMLNISK GPAVHSLRAQ ADKVRYSEVM RNVLENQEDL
YLRQIEVISL DIEDGKVKGI VTKNGACFTA NTIVLATGTY LRSRIIIGEV NYSGGPSGLF
PANELSQSLI DVGIKLRRFK TGTPARINKR SVDFSKMVEQ PGDERIIPFS FLNDKLEKEQ
ISCYLTYTNE KTHEVIKENI DRSPLYNGTI KSVGPRYCPS IEDKVMRFPD KQQHQIFIEP
EGENTNDLYV GGMSSSLPEE VQIKMLKTVP GLEDVEILKT AYAIEYDCID PTQLKLSLEF
KDVKGLFGAG QFNGSSGYEE AASQGIIAGI NAALMVKNKE PLILGRSDGY IGVLIDDLVT
KGTNEPYRMM TSRAEYRLLL RQDNADLRLT ELGHKIGLVD ENRYEKFIGR KNAIEEELNR
LKKVQITNKK EVNDFLEGLG SVSLKKPISL YELIRRPELD YDKLQTLDID RKDLAQDIID
EVNIMIKYEG YIEKQLEQVD QFKKFEKRVI PEDIDYNSIK NLRTEAIQKL SKLRPVNLGQ
ASRISGVSPS DISVLMIYLD YYFKNK