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MNMG_ACISJ
ID   MNMG_ACISJ              Reviewed;         661 AA.
AC   A1W207;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Ajs_0026;
OS   Acidovorax sp. (strain JS42).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax; unclassified Acidovorax.
OX   NCBI_TaxID=232721;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS42;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of chromosome 1 of Acidovorax sp. JS42.";
RL   Submitted (DEC-2006) 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; CP000539; ABM40282.1; -; Genomic_DNA.
DR   RefSeq; WP_011803498.1; NC_008782.1.
DR   AlphaFoldDB; A1W207; -.
DR   SMR; A1W207; -.
DR   STRING; 232721.Ajs_0026; -.
DR   EnsemblBacteria; ABM40282; ABM40282; Ajs_0026.
DR   KEGG; ajs:Ajs_0026; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_4; -.
DR   OMA; FRPGYAI; -.
DR   Proteomes; UP000000645; 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..661
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345234"
FT   BINDING         13..18
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         285..299
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   661 AA;  72628 MW;  A2C229085A891489 CRC64;
     MLYPQDFDVI VVGGGHAGTE AALAAARMGS RTLLLTHNIE TLGQMSCNPS IGGIGKGHLV
     KEVDALGGAM ALATDEAGIQ FRILNSSKGP AVRATRAQAD RILYKAAIRR MLENQPNLWL
     FQQAVDDLMV EGDRVVGAVT QVGIRFRSRA VVLTAGTFLD GKIHVGLNNY AAGRAGDPPA
     VSLSARLKEL QLPQGRLKTG TPPRIDGRSI DFSQCEEQPG DGMPGGVNEG QVPVFSFMAH
     AYGGAAMHPR QVPCWITHTN ARTHEIIRSG FDRSPMFTGK IEGVGPRYCP SVEDKINRFA
     DKESHQIFLE PEGLTTHEFY PNGISTSLPF DIQYDLVRSM HGLENAHILR PGYAIEYDYF
     DPRSLKSSFE TRQIQGLFFA GQINGTTGYE EAAAQGLFAG INAALQCRGV GAWVPARDEA
     YLGVLVDDLI TKGVTEPYRM FTSRAEFRLQ LREDNADMRL TEAGRRMGLV DDARWDAFSR
     KRDAVSRETE RLKSTWVNPR NLPTVEAERV LGKAIEHEYN LFDLLRRPDV GYDALTTMDG
     GKYASEAVSR ETLGELSASV IEQVEIAAKY AGYIDRQRDE VQRAAHFEKL RLPEDLDYMQ
     VAALSIEVRQ KLQKHRPETL GQASRISGVT PAAISLLMVH LKKGGFKGFA PQPADGVETV
     A
 
 
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