MNMG_BURPS
ID MNMG_BURPS Reviewed; 657 AA.
AC Q63PG8;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=BPSL3408;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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; BX571965; CAH37420.1; -; Genomic_DNA.
DR RefSeq; WP_004556009.1; NZ_CP009538.1.
DR RefSeq; YP_110001.1; NC_006350.1.
DR AlphaFoldDB; Q63PG8; -.
DR SMR; Q63PG8; -.
DR STRING; 272560.BPSL3408; -.
DR EnsemblBacteria; CAH37420; CAH37420; BPSL3408.
DR KEGG; bps:BPSL3408; -.
DR PATRIC; fig|272560.51.peg.1781; -.
DR eggNOG; COG0445; Bacteria.
DR OMA; FRPGYAI; -.
DR Proteomes; UP000000605; 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..657
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_0000117076"
FT REGION 636..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 657 AA; 71995 MW; 2187BF17E5A96F1B CRC64;
MLYPTEFDVI VVGGGHAGTE AALASARMGA KTLLLTHNIE TLGQMSCNPS IGGIGKGHLV
KEVDALGGAM AAATDEGGIQ FRILNSSKGP AVRATRAQAD RVLYKQAIRR RLENQPNLWL
FQQAVDDLMV EGDRVVGAVT QVGVRFRARA VVLTAGTFLD GKIHVGLNHY TGGRAGDPAA
VSLSSRLKEL NLPQGRLKTG TPPRIDGRTI DFSKLDEQPG DLDPIPVFSF LGRAEQHPQQ
LPCWVTHTNE RTHDIIRSGL DRSPMYTGVI EGVGPRYCPS IEDKIHRFAS KDSHQIFLEP
EGLTTNEFYP NGISTSLPFD VQLALVHSMR GLEQAHILRP GYAIEYDYFD PRALKSSLET
KAIGGLFFAG QINGTTGYEE AAAQGLLAGI NAGRYAQEKD AWCPRRDQAY LGVLVDDLVT
RGISEPYRMF TSRAEYRLSL REDNADMRLT EIGRELGVVD DVRWDAFNRK RDAVSRETER
LRTTWVTPKT LPADEATALL GKPIDHEYSL AELLRRPGVS YDGVCGLRGG ECGPSEPLAE
DELLLAQIKE QIEIGIKYQG YIERQAGEIE RNGANENTRL PDGIDYTEVR GLSFEVSQKL
NQFRPETIGQ ASRISGMTPA AISLLMVHLK KRGLGRRKGA DSVPGADVQA DNTAAQQ
