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