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MNMG_PARPJ
ID   MNMG_PARPJ              Reviewed;         652 AA.
AC   B2T7L1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=Bphyt_3905;
OS   Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS   (Burkholderia phytofirmans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=398527;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17436 / LMG 22146 / PsJN;
RX   PubMed=21551308; DOI=10.1128/jb.05055-11;
RA   Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J., Sessitsch A.;
RT   "Complete genome sequence of the plant growth-promoting endophyte
RT   Burkholderia phytofirmans strain PsJN.";
RL   J. Bacteriol. 193:3383-3384(2011).
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; CP001052; ACD18292.1; -; Genomic_DNA.
DR   RefSeq; WP_012434810.1; NC_010681.1.
DR   AlphaFoldDB; B2T7L1; -.
DR   SMR; B2T7L1; -.
DR   STRING; 398527.Bphyt_3905; -.
DR   EnsemblBacteria; ACD18292; ACD18292; Bphyt_3905.
DR   KEGG; bpy:Bphyt_3905; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_4; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000001739; 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; tRNA processing.
FT   CHAIN           1..652
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_1000095647"
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   652 AA;  71568 MW;  D81A6F385AA4158A CRC64;
     MLFPTEFDVI VVGGGHAGTE AALASARMGN TTLLLTHNIE TLGQMSCNPS IGGIGKGHLV
     KEVDALGGAM AAATDEGGIQ FRILNSSKGP AVRATRAQAD RLLYKQAIRH RLENQPNLWL
     FQQAVDDLMV EGDRVVGAVT QVGIRFRARA VVLTAGTFLD GKIHVGLNNY TGGRAGDPAA
     VSLSARLKEL KLPQGRLKTG TPPRIDGRTI DFSQLEEQPG DLDPVPVFSF LGRVEQHPRQ
     VPCWVTHTNE RTHDIIRGGL DRSPMYTGVI EGVGPRYCPS IEDKIHRFAS KESHQIFLEP
     EGLTTNEFYP NGISTSLPFD VQLELVRSMR GLEHAHILRP GYAIEYDYFD PRGLKASLET
     KVINGLFFAG QINGTTGYEE AAAQGLLAGI NAGLFVQGKE AWCPRRDQAY LGVLVDDLVT
     RGVSEPYRMF TSRAEYRLSL REDNADMRLT EIGRELGVVD DIRWDAFSRK RDAVSRETER
     LRTTWVNPKT LPADEATPLL GKPIDHEYSL ADLLRRPGVS YDGVCGLRAG ACAAPEALAE
     DDVLLAQIKE QIEIGIKYQG YIDRQAGEIE RNEAHESTRL PEGVDYAEVR GLSFEARQKL
     TQFRPETIGQ ASRISGITPA AISLLMVHLK RGLGRRPTKP AEPGADNKPV TQ
 
 
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