MNMG_LACLM
ID MNMG_LACLM Reviewed; 625 AA.
AC O32806; A2RMR7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 117.
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=llmg_2035;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-554.
RX PubMed=9226255; DOI=10.1128/jb.179.14.4473-4479.1997;
RA Duwat P., Cochu A., Ehrlich S.D., Gruss A.;
RT "Characterization of Lactococcus lactis UV-sensitive mutants obtained by
RT ISS1 transposition.";
RL J. Bacteriol. 179:4473-4479(1997).
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=AAC45494.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AM406671; CAL98603.1; -; Genomic_DNA.
DR EMBL; U80409; AAC45494.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; WP_011835755.1; NZ_WJVF01000004.1.
DR AlphaFoldDB; O32806; -.
DR SMR; O32806; -.
DR STRING; 416870.llmg_2035; -.
DR EnsemblBacteria; CAL98603; CAL98603; llmg_2035.
DR KEGG; llm:llmg_2035; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_9; -.
DR OMA; FRPGYAI; -.
DR PhylomeDB; O32806; -.
DR BioCyc; LLAC416870:LLMG_RS10175-MON; -.
DR Proteomes; UP000000364; 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..625
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_0000117118"
FT BINDING 13..18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 125
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 182
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 276..290
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 373
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT CONFLICT 542
FT /note="I -> S (in Ref. 2; AAC45494)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 625 AA; 69335 MW; F1DF471DACC948B6 CRC64;
MNFQENYDVI VIGGGHAGVE ASLAAARMGS KTLLMTINLN MVAFMPCNPS IGGSAKGIVV
REIDALGGEM GRNIDKTYIQ MKMLNTGKGP AVRALRAQAD KDEYAASMKN TVSDQENLTL
RQGMVEELIL DDEKQKVIGV RTSTGTQYGA KAVIITTGTA LRGEIIIGEL KYSSGPNNSL
SSIGLADNLR EIGFEIGRFK TGTPPRVLAS SIDYDKTEIQ PGDEAPNHFS FMSSDEDYLK
DQIPCWLTYT TENSHTILRD NLHRAPLFSG IVKGVGPRYC PSIEDKITRF ADKPRHQLFL
EPEGRNTEEV YIGGLSTSMP EDVQFDLVKS IPGLENAKMM RPGYAIEYDV VMPHQLRPTL
ETKLISGLFT AGQTNGTSGY EEAAGQGLVA GINAALKIQG KPEFILKRSE AYIGVMIDDL
VTKGTLEPYR LLTSRAEYRL ILRHDNADRR LTEIGRQVGL VSDAQWEHYQ AKMAQFDREM
KRLNSEKLKP LPDTQEKLGK LGFGPIKDAL TGAEFLKRPE VNYDEVIDFI GQAPEVIDRT
VIELIETEIT YEGYIKKAMD QVDKMHRLEA KRIPKNMDWD KLDSIATEAR QKFKKINPET
LGQASRISGV NPADISILMV YLEGK
