MNMG_BURM1
ID MNMG_BURM1 Reviewed; 656 AA.
AC A9AJF1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=Bmul_0093, BMULJ_03172;
OS Burkholderia multivorans (strain ATCC 17616 / 249).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=395019;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC
RT 17616.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA Hattori M., Tsuda M.;
RT "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL Submitted (APR-2007) 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; CP000868; ABX13788.1; -; Genomic_DNA.
DR EMBL; AP009385; BAG45046.1; -; Genomic_DNA.
DR RefSeq; WP_012212470.1; NC_010804.1.
DR AlphaFoldDB; A9AJF1; -.
DR SMR; A9AJF1; -.
DR STRING; 395019.Bmul_0093; -.
DR EnsemblBacteria; BAG45046; BAG45046; BMULJ_03172.
DR KEGG; bmj:BMULJ_03172; -.
DR KEGG; bmu:Bmul_0093; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_4; -.
DR OMA; FRPGYAI; -.
DR Proteomes; UP000008815; Chromosome 1.
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..656
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_1000095645"
FT BINDING 13..18
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 656 AA; 71886 MW; D4C2A22D67129F3B CRC64;
MLYPTEFDVI VVGGGHAGTE AALASARMGA KTLLLTHNIE TLGQMSCNPS IGGIGKGHLV
KEVDALGGAM AAATDEAGIQ FRILNSSKGP AVRATRAQAD RILYKAAIRR RLENQPNLWL
FQQAVDDLMV EGDCVVGAVT QIGIRFRARA VVLTAGTFLD GKIHVGLNNY TGGRAGDPAA
VSLSARLKEL KLPQGRLKTG TPPRIDGRTI DFSKLEEQPG DLDPIPVFSF LGRAEQHPQQ
LPCWVTHTNE RTHDIIRGGL DRSPMYTGVI EGVGPRYCPS IEDKIHRFAS KESHQIFLEP
EGLTTNEFYP NGISTSLPFD VQLELVHSMR GLEQAHILRP GYAIEYDYFD PRALKASLET
KAINGLFFAG QINGTTGYEE AAAQGLLAGV NAGRYVQEKD AWCPRRDQAY LGVLVDDLVT
RGVAEPYRMF TSRAEYRLSL REDNADMRLT EIGRELGLVD DVRWDAFCRK RDAVSRETER
LKTTWVTPKT LPPEEATALL GKPIDHEYSL AELLRRPGVD YDGVCGLKGG ECGPAEPLAD
DPVLLAQIKE QVEIGIKYQG YIERQATEIE RNDANENTRL PDGIDYREVR GLSFEVSQKL
NQFRPETIGQ ASRISGVTPA AISLLMVHLK RRGLGRRNGA AAPAAEQGDG AVPTQQ